Displaying publications 41 - 60 of 231 in total

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  1. Chow YH, Yap YJ, Anuar MS, Tejo BA, Ariff A, Show PL, et al.
    PMID: 23911538 DOI: 10.1016/j.jchromb.2013.06.034
    A relationship is proposed for the interfacial partitioning of protein in poly(ethylene glycol) (PEG)-phosphate aqueous two-phase system (ATPS). The relationship relates the natural logarithm of interfacial partition coefficient, ln G to the PEG concentration difference between the top and bottom phases, Δ[PEG], with the equation ln G=AΔ[PEG]+B. Results showed that this relationship provides good fits to the partition of bovine serum albumin (BSA) in ATPS which is comprised of phosphate and PEG of four different molecular weight 1450g/mol, 2000g/mol, 3350g/mol and 4000g/mol, with the tie-line length (TLL) in the range of 44-60% (w/w) at pH 7.0. The decrease of A values with the increase of PEG molecular weight indicates that the correlation between ln G and Δ[PEG] decreases with the increase in PEG molecular weight and the presence of protein-polymer hydrophobic interaction. When temperature was increased, a non-linear relationship of ln G inversely proportional to temperature was observed. The amount of proteins adsorbed at the interface increased proportionally with the amount of BSA loaded whereas the partition coefficient, K remained relatively constant. The relationship proposed could be applied to elucidate interfacial partitioning behaviour of other biomolecules in polymer-salt ATPS.
    Matched MeSH terms: Serum Albumin, Bovine/isolation & purification; Serum Albumin, Bovine/chemistry*
  2. Govindasamy V, Ronald VS, Abdullah AN, Ganesan Nathan KR, Aziz ZA, Abdullah M, et al.
    Cytotherapy, 2011 Nov;13(10):1221-33.
    PMID: 21929379 DOI: 10.3109/14653249.2011.602337
    BACKGROUND AIMS. Dental pulp stromal cells (DPSC) are considered to be a promising source of stem cells in the field of regenerative therapy. However, the usage of DPSC in transplantation requires large-scale expansion to cater for the need for clinical quantity without compromising current good manufacturing practice (cGMP). Existing protocols for cell culturing make use of fetal bovine serum (FBS) as a nutritional supplement. Unfortunately, FBS is an undesirable additive to cells because it carries the risk of transmitting viral and prion diseases. Therefore, the present study was undertaken to examine the efficacy of human platelet lysate (HPL) as a substitute for FBS in a large-scale set-up. METHODS. We expanded the DPSC in Dulbecco's modified Eagle's medium-knock-out (DMEM-KO) with either 10% FBS or 10% HPL, and studied the characteristics of DPSC at pre- (T25 culture flask) and post- (5-STACK chamber) large-scale expansion in terms of their identity, quality, functionality, molecular signatures and cytogenetic stability. RESULTS. In both pre- and post-large-scale expansion, DPSC expanded in HPL showed extensive proliferation of cells (c. 2-fold) compared with FBS; the purity, immune phenotype, colony-forming unit potential and differentiation were comparable. Furthermore, to understand the gene expression profiling, the transcriptomes and cytogenetics of DPSC expanded under HPL and FBS were compared, revealing similar expression profiles. CONCLUSIONS. We present a highly economized expansion of DPSC in HPL, yielding double the amount of cells while retaining their basic characteristics during a shorter time period under cGMP conditions, making it suitable for therapeutic applications.
    Matched MeSH terms: Culture Media, Serum-Free/pharmacology*; Culture Media, Serum-Free/chemistry; Serum/metabolism
  3. Yunus MH, Siang KC, Hashim NI, Zhi NP, Zamani NF, Sabri PP, et al.
    Tissue Cell, 2014 Aug;46(4):233-40.
    PMID: 24973262 DOI: 10.1016/j.tice.2014.05.003
    The culture of human airway epithelial cells has played an important role in advancing our understanding of the metabolic and molecular mechanisms underlying normal function and disease pathology of airway epithelial cells. The present study focused on investigating the effects of human serum (HS) on the qualitative and quantitative properties of the human respiratory epithelium compared to the fetal bovine serum (FBS), as a supplement in culture. Respiratory epithelial (RE) cells derived from human nasal turbinate were co-cultured with fibroblasts, subsequently separated at 80-90% confluency by differential trypsinization. RE cells were then sub-cultured into 2 different plates containing 5% allogenic HS and FBS supplemented media respectively up to passage 1 (P1). Cell morphology, growth rate, cell viability and population doubling time were assessed under light microscope, and levels of gene expression were measured via real time reverse transcriptase-polymerase chain reaction (qRT-PCR). RE cells appeared as polygonal shape and expanded when cultured in HS whereas RE cells in FBS were observed to be easily matured thus limit the RE cells expansion. Proliferation rate of RE cells in HS supplemented media (7673.18 ± 1207.15) was 3 times higher compared to RE in FBS supplemented media (2357.68 ± 186.85). Furthermore, RE cells cultured in HS-supplemented media required fewer days (9.15 ± 1.10) to double in numbers compared to cells cultured in FBS-supplemented media (13.66 ± 0.81). Both the differences were significant (p<0.05). However, there were no significant differences in the viability of RE cells in both groups (p=0.105). qRT-PCR showed comparable expressions of gene Cytokeratin-14 (CK-14), Cytokeratin-18 (CK-18) and Mucin-5 subtype B (MUC5B) in RE cells cultured in both groups (p>0.05). In conclusion, HS is a comparatively better choice of media supplement in accelerating growth kinetics of RE cells in vitro thus producing a better quality of respiratory epithelium for future tracheal reconstruction.
    Matched MeSH terms: Serum/metabolism*; Serum/chemistry
  4. Wan-Ibrahim WI, Ashrafzadeh A, Singh VA, Hashim OH, Abdul-Rahman PS
    Electrophoresis, 2016 09;37(17-18):2328-37.
    PMID: 27062367 DOI: 10.1002/elps.201500522
    Sarcoma is a malignant tumor that originates from the bone or soft tissue. In this study, abundances of serum amyloid A (SAA) in patients with pleomorphic sarcoma (PS), chondrosarcoma (CS), and osteosarcoma (OS) were analyzed and compared with those from their respective age-matched healthy control subjects. Results obtained from our analysis by 2DE showed that the levels of SAA were markedly elevated in patients with PS and OS, which are highly metastatic, while in patients with CS, which is a less aggressive sarcoma, the increase appeared less pronounced. A similar trend of altered abundances was also observed when the levels of SAA in the subjects were estimated using Western blot, ELISA, and multiple-reaction monitoring analyses. Absolute quantification using multiple-reaction monitoring further demonstrated that the increased abundance of SAA in patients with PS, OS, and CS was mainly attributed to isoform SAA1. In view of the different degrees of tumor malignancy in PS, OS, and CS, our data suggest their apparent correlation with the levels of SAA in the patients.
    Matched MeSH terms: Serum Amyloid A Protein/metabolism*; Serum Amyloid A Protein/chemistry
  5. Kabir MZ, Mukarram AK, Mohamad SB, Alias Z, Tayyab S
    J. Photochem. Photobiol. B, Biol., 2016 Jul;160:229-39.
    PMID: 27128364 DOI: 10.1016/j.jphotobiol.2016.04.005
    Interaction of a promising anticancer drug, lapatinib (LAP) with the major transport protein in human blood circulation, human serum albumin (HSA) was investigated using fluorescence and circular dichroism (CD) spectroscopy as well as molecular docking analysis. LAP-HSA complex formation was evident from the involvement of static quenching mechanism, as revealed by the fluorescence quenching data analysis. The binding constant, Ka value in the range of 1.49-1.01×10(5)M(-1), obtained at three different temperatures was suggestive of the intermediate binding affinity between LAP and HSA. Thermodynamic analysis of the binding data (∆H=-9.75kJmol(-1) and ∆S=+65.21Jmol(-1)K(-1)) suggested involvement of both hydrophobic interactions and hydrogen bonding in LAP-HSA interaction, which were in line with the molecular docking results. LAP binding to HSA led to the secondary and the tertiary structural alterations in the protein as evident from the far-UV and the near-UV CD spectral analysis, respectively. Microenvironmental perturbation around Trp and Tyr residues in HSA upon LAP binding was confirmed from the three-dimensional fluorescence spectral results. LAP binding to HSA improved the thermal stability of the protein. LAP was found to bind preferentially to the site III in subdomain IB on HSA, as probed by the competitive drug displacement results and supported by the molecular docking results. The effect of metal ions on the binding constant between LAP and HSA was also investigated and the results showed a decrease in the binding constant in the presence of these metal ions.
    Matched MeSH terms: Serum Albumin/metabolism*; Serum Albumin/chemistry
  6. Ahmad N, Amin MC, Mahali SM, Ismail I, Chuang VT
    Mol Pharm, 2014 Nov 3;11(11):4130-42.
    PMID: 25252107 DOI: 10.1021/mp5003015
    Stimuli-responsive bacterial cellulose-g-poly(acrylic acid) hydrogels were investigated for their potential use as an oral delivery system for proteins. These hydrogels were synthesized using electron beam irradiation without any cross-linking agents, thereby eliminating any potential toxic effects associated with cross-linkers. Bovine serum albumin (BSA), a model protein drug, was loaded into the hydrogels, and the release profile in simulated gastrointestinal fluids was investigated. Cumulative release of less than 10% in simulated gastric fluid (SGF) demonstrated the potential of these hydrogels to protect BSA from the acidic environment of the stomach. Subsequent conformational stability analyses of released BSA by SDS-PAGE, circular dichroism, and an esterase activity assay indicated that the structural integrity and bioactivity of BSA was maintained and preserved by the hydrogels. Furthermore, an increase in BSA penetration across intestinal mucosa tissue was observed in an ex vivo penetration experiment. Our fabricated hydrogels exhibited excellent cytocompatibility and showed no sign of toxicity, indicating the safety of these hydrogels for in vivo applications.
    Matched MeSH terms: Serum Albumin, Bovine/administration & dosage*; Serum Albumin, Bovine/chemistry*
  7. Sonthanasamy RSA, Sulaiman NMN, Tan LL, Lazim AM
    PMID: 30954801 DOI: 10.1016/j.saa.2019.03.108
    Carbon dots (C-dots) were used to study the binding mechanisms with serum protein, bovine serum albumin (BSA) by using two notable binding systems known as non-covalent and covalent interaction. Interaction between C-dots and BSA were estimated by Stern-Volmer equation and Double Log Regression Model (DLRM). According to the fluorescent intensity, quenching of model carrier protein by C-dots was due to dynamic quenching for non-covalent and static quenching for covalent binding. The binding site constant, KA and number of binding site, for covalent interaction is 1754.7L/mol and n≈1 (0.6922) were determined by DLRM on fluorescence quenching results. The blue shift of the fluorescence spectrum, from 450nm to 421nm (non-covalent) and 430nm (covalent) and suggested that both the microenvironment of C-dots and protein changed in relation to the protein concentration. The fluorescence intensity results show that protein structure has a significant role in Protein-C-dots interactions and type of binding influence physicochemical properties of C-dots differently. Understanding to this bio interface is important to utilize both quantum dots and biomolecules for biomedical field. It can be a useful guideline to design further applications in biomedical and bioimaging.
    Matched MeSH terms: Serum Albumin, Bovine/metabolism*; Serum Albumin, Bovine/chemistry
  8. Said N, Khoo YS, Lau WJ, Gürsoy M, Karaman M, Ting TM, et al.
    Membranes (Basel), 2020 Dec 07;10(12).
    PMID: 33297433 DOI: 10.3390/membranes10120401
    In this work, several ultrafiltration (UF) membranes with enhanced antifouling properties were fabricated using a rapid and green surface modification method that was based on the plasma-enhanced chemical vapor deposition (PECVD). Two types of hydrophilic monomers-acrylic acid (AA) and 2-hydroxyethyl methacrylate (HEMA) were, respectively, deposited on the surface of a commercial UF membrane and the effects of plasma deposition time (i.e., 15 s, 30 s, 60 s, and 90 s) on the surface properties of the membrane were investigated. The modified membranes were then subjected to filtration using 2000 mg/L pepsin and bovine serum albumin (BSA) solutions as feed. Microscopic and spectroscopic analyses confirmed the successful deposition of AA and HEMA on the membrane surface and the decrease in water contact angle with increasing plasma deposition time strongly indicated the increase in surface hydrophilicity due to the considerable enrichment of the hydrophilic segment of AA and HEMA on the membrane surface. However, a prolonged plasma deposition time (>15 s) should be avoided as it led to the formation of a thicker coating layer that significantly reduced the membrane pure water flux with no significant change in the solute rejection rate. Upon 15-s plasma deposition, the AA-modified membrane recorded the pepsin and BSA rejections of 83.9% and 97.5%, respectively, while the HEMA-modified membrane rejected at least 98.5% for both pepsin and BSA. Compared to the control membrane, the AA-modified and HEMA-modified membranes also showed a lower degree of flux decline and better flux recovery rate (>90%), suggesting that the membrane antifouling properties were improved and most of the fouling was reversible and could be removed via simple water cleaning process. We demonstrated in this work that the PECVD technique is a promising surface modification method that could be employed to rapidly improve membrane surface hydrophilicity (15 s) for the enhanced protein purification process without using any organic solvent during the plasma modification process.
    Matched MeSH terms: Serum Albumin, Bovine
  9. George-Kodiseri E, Faridah K, Mariam S
    Family Physician, 1989;1:31-33.
    Anaemia is present in 31.3% of male and 73.6% of female subjects heterogenous for beta thalassaemia. In males, none had serum ferritin (SF) levels less than 10 ng/ml. In contrast, female subjects with haemoglobins less than 12 gm/dl, had SF levels less than 20 ng/ml. Statistical differences in the Hb, RBC, MCV, MCH, MCHC abd HBA were found with the normal groups (p<0.001). Comparison of the SF levels in both the males and females show no difference from those in the normal groups (p<0.10). Iron loading was not a significant feature in both the males and females. Correlation of the SF with age shows a weak negative correlation. Married females with children showed that the SF levels fell significantly with increasing age, suggesting the possibility that repeated pregnancies may deplete iron stores as reflected by the SF levels. In countries where iron deficiency and thalassaemia are highly prevalent, assays of serum ferittin will indicate if there is a need for supplemental iron in subjects hetergenous for beta thalassaemia.
    Matched MeSH terms: Serum
  10. Sharif SP, Friedmacher F, Amin A, Zaki RA, Hird MF, Khashu M, et al.
    J Pediatr Surg, 2020 Dec;55(12):2625-2629.
    PMID: 32771214 DOI: 10.1016/j.jpedsurg.2020.07.003
    PURPOSE: To investigate whether serum albumin (SA) concentration can predict the need for surgical intervention in neonates with necrotizing enterocolitis (NEC).

    METHODS: Retrospective review of all cases with NEC Bell's stage 2 and 3 that were treated in a single center between 2009 and 2015. Data on patient demographics, clinical parameters, laboratory findings and surgical status were recorded. Receiver operating characteristics analysis was used to evaluate optimal cutoffs and predictive values.

    RESULTS: Overall, 151 neonates with NEC were identified. Of these, 132 (87.4%) had confirmed NEC Bell's stage 2. The median gestational age was 28.4 (range, 23.1-39.0) weeks and 69 (52.3%) had a birth weight of ≤1000 g. Sixty-eight (51.5%) underwent surgery, showing a sustained reduction in SA over time with significantly lower median SA levels compared to 64 (48.5%) cases that responded well to medical treatment (18.3 ± 3.7 g/L vs. 26.0 ± 2.0 g/L; P 

    Matched MeSH terms: Serum Albumin
  11. Noor Aini Mohd. Yusoff, Zalina Abu Zaid, Raiza Sham, Rosita Jamaluddin, Suzana Shahar, A. Rahman A. Jamal
    MyJurnal
    Malnutrition is common among pediatric oncology patients. Factors contributing to malnutrition include physiological abnormalities, response to the tumors and side effects of the treatment. A pilot study was carried out to determine the nutritional status of 17 pediatric oncology patients aged 4 to 12 years old in Hospital Universiti Kebangsaan Malaysia, Kuala Lumpur. The
    nutritional status was assessed via anthropometric measurements and dietary intake through 3 days repeatitive 24 hours diet recall with subjects and their carers. Biochemical profiles (serum albumin and hemoglobin) were reviewed from the medical record. Through anthropometry measurements, weight and height were used to calculate Z-scores and further determine the percentile weight-for-age, height-for-age using NCHS percentile charts (WHO 1983). Frisancho’s standards (1981) were used to define malnutrition based on MUACfor- age. Underweight as determined using z scores below -2 for weight-for-age was observed in 70.6% of the subjects. Whilst, 76.5% of the subjects were classified as stunted (z score < –2) for height-for-age. Based on MUAC-for-age percentile, the sign of severe malnutrition category (<5 percentile) was observed in 35.3% of the subject and 23.6% of the subject were in the moderate malnutrition (>5 – <10 percentile). About 70.6% of the subject had low haemoglobin (< 11 g/dl) and 29.4% of the subject were hypoalbuminemia (< 35 g/dl) . Total macronutrient intake was assessed and compared with the individual requirement (Seashore 1984) for energy and protein intake were satisfactory, except for subjects in age group 10 – 12 years who achieved only 70% of the individuals requirements. As a conclusion, although food intake of the subjects was satisfactory but chronic malnutrition was prevalent. Early recognition of malnutrition is essential in order to plan for a nutritional intervention and further enhancing the quality of life.
    Key words: Nutritional status, pediatric oncology, anthropometric, dietary intake, biochemical profile.
    Matched MeSH terms: Serum Albumin
  12. Arapidi G, Osetrova M, Ivanova O, Butenko I, Saveleva T, Pavlovich P, et al.
    Data Brief, 2018 Jun;18:1204-1211.
    PMID: 29900295 DOI: 10.1016/j.dib.2018.04.018
    Blood as connective tissue potentially contains evidence of all processes occurring within the organism, at least in trace amounts (Petricoin et al., 2006) [1]. Because of their small size, peptides penetrate cell membranes and epithelial barriers more freely than proteins. Among the peptides found in blood, there are both fragments of proteins secreted by various tissues and performing their function in plasma and receptor ligands: hormones, cytokines and mediators of cellular response (Anderson et al., 2002) [2]. In addition, in minor amounts, there are peptide disease markers (for example, oncomarkers) and even foreign peptides related to pathogenic organisms and infection agents. To propose an approach for detailed peptidome characterization, we carried out an LC-MS/MS analysis of blood serum and plasma samples taken from 20 healthy donors on a TripleTOF 5600+ mass-spectrometer. We prepared samples based on our previously developed method of peptide desorption from the surface of abundant blood plasma proteins followed by standard chromatographic steps (Ziganshin et al., 2011) [3]. The mass-spectrometry peptidomics data presented in this article have been deposited to the ProteomeXchange Consortium (Deutsch et al., 2017) [4] via the PRIDE partner repository with the dataset identifier PXD008141 and 10.6019/PXD008141.
    Matched MeSH terms: Serum
  13. Siti Yazmin Zahari Sham, Subashini C. Thambiah, Intan Nureslyna Samsudin
    MyJurnal
    Free light chains (FLCs) are tumour markers of monoclonal gammopathies. Detection of urinary FLC or also known as Bence-Jones protein through urinary protein and its immunofixation electrophoreses (UPE and uIFE, respectively) have been considered the gold standard for its biochemical diagnosis. This is mainly due to their superior detection limits compared to their counterpart investigations in serum. However, urinalysis is limited in many ways. The emergence of serum FLC assay with markedly improved detection limit circumvents many of these problems and has gained much importance in biochemical investigations of monoclonal gammopathies. Nevertheless, they are not without limitations. This review discusses the advantages and limitations of serum and urinary FLC assays.
    Matched MeSH terms: Serum
  14. Landor JV
    DOI: 10.1016/S0035-9203(41)90065-2
    1. (1) The injection of serum prepared especially against strains of typhoid bacilli strong in "O" and "Vi" antigens appeared during the epidemic at Singapore to be of value in the treatment of serious cases of typhoid fever, even at a comparatively late stage of the disease. The time for the routine use of such serum in treatment has perhaps not yet come, but strong indications for its use are severe toxaemia, or failure to improve with general treatment. 2. (2) The absence of eosinophil cells in a differential white blood count is of value in the diagnosis though it is not an absolute sign in either a negative or positive direction. 3. (3) Congenital immunity against typhoid fever appears to be powerful for several years of childhood, in Malaya and presumably elsewhere also. 4. (4) Compulsory inoculation is advocated as a public health measure of protection against typhoid fever in countries where the disease is endemic, but not earlier than the 5th year of age. c 1941
    Matched MeSH terms: Serum
  15. Amjad MW, Mohd Amin MC, Mahali SM, Katas H, Ismail I, Hassan MN, et al.
    PLoS One, 2014;9(8):e105234.
    PMID: 25133390 DOI: 10.1371/journal.pone.0105234
    Biomolecules have been widely investigated as potential therapeutics for various diseases. However their use is limited due to rapid degradation and poor cellular uptake in vitro and in vivo. To address this issue, we synthesized a new nano-carrier system comprising of cholic acid-polyethylenimine (CA-PEI) copolymer micelles, via carbodiimide-mediated coupling for the efficient delivery of small interfering ribonucleic acid (siRNA) and bovine serum albumin (BSA) as model protein. The mean particle size of siRNA- or BSA-loaded CA-PEI micelles ranged from 100-150 nm, with zeta potentials of +3-+11 mV, respectively. Atomic force, transmission electron and field emission scanning electron microscopy demonstrated that the micelles exhibited excellent spherical morphology. No significant morphology or size changes were observed in the CA-PEI micelles after siRNA and BSA loading. CA-PEI micelles exhibited sustained release profile, the effective diffusion coefficients were successfully estimated using a mathematically-derived cylindrical diffusion model and the release data of siRNA and BSA closely fitted into this model. High siRNA and BSA binding and loading efficiencies (95% and 70%, respectively) were observed for CA-PEI micelles. Stability studies demonstrated that siRNA and BSA integrity was maintained after loading and release. The CA-PEI micelles were non cytotoxic to V79 and DLD-1 cells, as shown by alamarBlue and LIVE/DEAD cell viability assays. RT-PCR study revealed that siRNA-loaded CA-PEI micelles suppressed the mRNA for ABCB1 gene. These results revealed the promising potential of CA-PEI micelles as a stable, safe, and versatile nano-carrier for siRNA and the model protein delivery.
    Matched MeSH terms: Serum Albumin, Bovine/chemistry
  16. Feroz SR, Mohamad SB, Bujang N, Malek SN, Tayyab S
    J Agric Food Chem, 2012 Jun 13;60(23):5899-908.
    PMID: 22624666 DOI: 10.1021/jf301139h
    Interaction of flavokawain B (FB), a multitherapeutic flavonoid from Alpinia mutica with the major transport protein, human serum albumin (HSA), was investigated using different spectroscopic probes, i.e., intrinsic, synchronous, and three-dimensional (3-D) fluorescence, circular dichroism (CD), and molecular modeling studies. Values of binding parameters for FB-HSA interaction in terms of binding constant and stoichiometry of binding were determined from the fluorescence quench titration and were found to be 6.88 × 10(4) M(-1) and 1.0 mol of FB bound per mole of protein, respectively, at 25 °C. Thermodynamic analysis of the binding data obtained at different temperatures showed that the binding process was primarily mediated by hydrophobic interactions and hydrogen bonding, as the values of the enthalpy change (ΔH) and the entropy change (ΔS) were found to be -6.87 kJ mol(-1) and 69.50 J mol(-1) K(-1), respectively. FB binding to HSA led to both secondary and tertiary structural alterations in the protein as revealed by intrinsic, synchronous, and 3-D fluorescence results. Increased thermal stability of HSA in the presence of FB was also evident from the far-UV CD spectral results. The distance between the bound ligand and Trp-214 of HSA was determined as 3.03 nm based on the Förster resonance energy transfer mechanism. Displacement experiments using bilirubin and warfarin coupled with molecular modeling studies assigned the binding site of FB on HSA at domain IIA, i.e., Sudlow's site I.
    Matched MeSH terms: Serum Albumin/metabolism*
  17. Gan CY, Alkarkhi AF, Easa AM
    J Biosci Bioeng, 2009 Apr;107(4):366-72.
    PMID: 19332294 DOI: 10.1016/j.jbiosc.2008.12.007
    D-optimal design was employed to optimize the mixture of cross-linking agents formulation: microbial transglutaminase (MTGase) and ribose, and the processing parameters (i.e. incubation and heating time) in the mixture in order to obtain combined-cross-linked bovine serum albumin gels that have high gel strength, pH close to neutral and yet medium in browning. Analysis of variance (ANOVA) showed that the contribution of quadratic term to the model over the linear was significant for pH and L* value, whereas linear model was significant for gel strength. Optimization study using response surface methodology (RSM) was performed to the mixture components and process variables and the optimum conditions obtained were: MTGase of 1.34-1.43 g/100 mL, ribose of 1.07-1.16 g/100 mL, incubation time of 5 h at 40 degrees C and heating time of 3 h at 90 degrees C.
    Matched MeSH terms: Serum Albumin, Bovine/chemistry*
  18. Yeo CK, Hapizah MN, Khalid BAK, Wan Nazainimoon WM, Khalid Y
    Med J Malaysia, 2004 Jun;59(2):185-9.
    PMID: 15559168
    Diabetes mellitus is an important coronary artery disease risk factor. The presence of microalbuminuria, which indicates renal involvement in diabetic patients, is associated with an increased cardiovascular risk. There are suggestions that diabetic patients with microalbuminuria have more adverse risk profile such as higher ambulatory blood pressure and total cholesterol levels to account for the increased cardiovascular morbidity and mortality. QT dispersion is increasingly being recognized as a prognostic factor for coronary artery disease and sudden death. Some studies have suggested that QT dispersion is an important predictor of mortality in Type II diabetic patients. Our cross sectional study was to compare the QT dispersion and 24 hour ambulatory blood pressure monitoring between diabetic patients with microalbuminuria and those without microalbuminuria. Diabetic patients with overt coronary artery disease were excluded from the study. A total of 108 patients were recruited of which 57 patients had microalbuminuria and 51 were without microalbuminuria. The mean value of QT dispersion was significantly higher in patients with microalbuminuria than in patients without microalbuminuria (58.9 +/- 27.9 ms vs. 47.1 +/- 25.0 ms, p < 0.05). The mean 24 hour systolic and diastolic blood pressures were significantly higher in patients with microalbuminuria than in patients without microalbuminuria (129.5 +/- 12.3 mm Hg vs 122.3 +/- 10.2 mm Hg, p < 0.05 and 78.4 +/- 6.9 mm Hg vs 75.3 +/- 6.8 mm Hg, p < 0.05, respectively). Our study suggests that QT dispersion prolongation, related perhaps to some autonomic dysfunction, is an early manifestation of cardiovascular aberration in diabetic patients with microalbuminuria. The higher blood pressure levels recorded during a 24-hour period min diabetics with microalbuminuria could also possibly account for the worse cardiovascular outcome in this group of patients.
    Matched MeSH terms: Serum Albumin/analysis*
  19. Azmi B, Aminuddin BS, Sharaf I, Samsudin OC, Munirah S, Chua KH, et al.
    Med J Malaysia, 2004 May;59 Suppl B:13-4.
    PMID: 15468795
    Animal serum is commonly used in chondrocytes culture expansion to promote cell proliferation and shorten the time lag before new tissue reconstruction is possible. However, animal serum is not suitable for regeneration of clinical tissue because it has potential risk of viral and prion related disease transmission particularly mad cow disease and foreign protein contamination that can stimulate immune reaction leading to graft rejection. In this context, human serum as homologous supplement has a greater potential as growth promoting agents for human chondrocytes culture.
    Matched MeSH terms: Serum*
  20. Badrul AH, Aminuddin BS, Sharaf I, Samsudin OC, Munirah S, Ruszymah BH
    Med J Malaysia, 2004 May;59 Suppl B:11-2.
    PMID: 15468794
    Culture media supplemented with animal serum e.g. fetal bovine serum; FBS is commonly used for human culture expansion. However, for clinical application, FBS is restricted as its carry a risk of viral or prion transmission. Engineering autologous cartilage with autologous human serum supplementation is seen as a better solution to reduce the risk of transmitting infectious diseases and immune rejection during cartilage transplantation. The purpose of this study is to establish and compare the effects of 10% autologous human serum (AHS) and 10% FBS on the growth of chondrocytes and the formation of tissue engineered human articular cartilage.
    Matched MeSH terms: Serum*
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