Displaying publications 1 - 20 of 230 in total

  1. Al-Joudi FS, Wahab NA
    Med J Malaysia, 2004 Oct;59(4):495-501.
    PMID: 15779582 MyJurnal
    The albumin globulin ratio (A/G ratio) is meant to represent the ratio of alterations in serum proteins, since, in liver disease, globulins (G) rise following serum albumin (SA) decrease. pathophysiological value, its' use has been limited. Alternatively, we have developed an index, the globulin compensation index (GCI) to measure the changes in serum globulins when albumin is decreased. The index is calculated as follows: G - 25 / 35 - SA. The GCI has been tested using retrospective patients' data from the Hospital Universiti Sains Malaysia. Analysis of the data shows that the GCI may be of potential value in showing the actual serum protein status, especially in cases where globulins are decreased along with albumin. Furthermore, globulin rise in cases with reduced albumin was found in 72.3% of cases of hepatic diseases, whereas this finding occurred in up to 32.3% of cases of non-hepatic, systemic diseases.
    Matched MeSH terms: Serum Albumin/analysis*; Serum Globulins/analysis*
  2. George E, Faridah K
    Family Practitioner, 1986;9:38-40.
    Matched MeSH terms: Serum
  3. Lee PY, Osman J, Low TY, Jamal R
    Bioanalysis, 2019 Oct;11(19):1799-1812.
    PMID: 31617391 DOI: 10.4155/bio-2019-0145
    Plasma and serum are widely used for proteomics-based biomarker discovery. However, analysis of these biofluids is highly challenging due to the complexity and wide dynamic range of their proteomes. Notably, highly abundant proteins tend to obscure the detection of potential biomarkers that are usually of lower concentrations. Among the strategies to resolve this problem are: depletion of high-abundance proteins, enrichment of low abundant proteins of interest and prefractionation. In this review, we focus on current and emerging depletion techniques used to enhance the detection and identification of the less abundant proteins in plasma and serum. We discuss the applications and contributions of these methods to proteomics analysis of plasma and serum alongside their limitations and future perspectives.
    Matched MeSH terms: Serum
  4. VELLA F
    Med J Malaya, 1957 Dec;12(2):456-63.
    PMID: 13515878
    Matched MeSH terms: Serum Globulins*
  5. Chow YH, Yap YJ, Tan CP, Anuar MS, Tejo BA, Show PL, et al.
    J Biosci Bioeng, 2015 Jul;120(1):85-90.
    PMID: 25553974 DOI: 10.1016/j.jbiosc.2014.11.021
    In this paper, a linear relationship is proposed relating the natural logarithm of partition coefficient, ln K for protein partitioning in poly (ethylene glycol) (PEG)-phosphate aqueous two-phase system (ATPS) to the square of tie-line length (TLL(2)). This relationship provides good fits (r(2) > 0.98) to the partition of bovine serum albumin (BSA) in PEG (1450 g/mol, 2000 g/mol, 3350 g/mol, and 4000 g/mol)-phosphate ATPS with TLL of 25.0-50.0% (w/w) at pH 7.0. Results also showed that the plot of ln K against pH for BSA partitioning in the ATPS containing 33.0% (w/w) PEG1450 and 8.0% (w/w) phosphate with varied working pH between 6.0 and 9.0 exhibited a linear relationship which is in good agreement (r(2) = 0.94) with the proposed relationship, ln K = α' pH + β'. These results suggested that both the relationships proposed could be applied to correlate and elucidate the partition behavior of biomolecules in the polymer-salt ATPS. The influence of other system parameters on the partition behavior of BSA was also investigated. An optimum BSA yield of 90.80% in the top phase and K of 2.40 was achieved in an ATPS constituted with 33.0% (w/w) PEG 1450 and 8.0% (w/w) phosphate in the presence of 8.5% (w/w) sodium chloride (NaCl) at pH 9.0 for 0.3% (w/w) BSA load.
    Matched MeSH terms: Serum Albumin, Bovine/isolation & purification; Serum Albumin, Bovine/chemistry*
  6. Migasena P, Maegraith BG
    Med J Malaya, 1968 Mar;22(3):251.
    PMID: 4234389
    Matched MeSH terms: Serum Albumin/metabolism*; Serum Albumin, Radio-Iodinated
  7. Campana M, Hosking SL, Petkov JT, Tucker IM, Webster JR, Zarbakhsh A, et al.
    Langmuir, 2015 May 26;31(20):5614-22.
    PMID: 25875917 DOI: 10.1021/acs.langmuir.5b00646
    The structure of the adsorbed protein layer at the oil/water interface is essential to the understanding of the role of proteins in emulsion stabilization, and it is important to glean the mechanistic events of protein adsorption at such buried interfaces. This article reports on a novel experimental methodology for probing protein adsorption at the buried oil/water interface. Neutron reflectivity was used with a carefully selected set of isotopic contrasts to study the adsorption of bovine serum albumin (BSA) at the hexadecane/water interface, and the results were compared to those for the air/water interface. The adsorption isotherm was determined at the isoelectric point, and the results showed that a higher degree of adsorption could be achieved at the more hydrophobic interface. The adsorbed BSA molecules formed a monolayer on the aqueous side of the interface. The molecules in this layer were partially denatured by the presence of oil, and once released from the spatial constraint by the globular framework they were free to establish more favorable interactions with the hydrophobic medium. Thus, a loose layer extending toward the oil phase was clearly observed, resulting in an overall broader interface. By analogy to the air/water interface, as the concentration of BSA increased to 1.0 mg mL(-1) a secondary layer extending toward the aqueous phase was observed, possibly resulting from the steric repulsion upon the saturation of the primary monolayer. Results clearly indicate a more compact arrangement of molecules at the oil/water interface: this must be caused by the loss of the globular structure as a consequence of the denaturing action of the hexadecane.
    Matched MeSH terms: Serum Albumin, Bovine/chemistry*
  8. Wong YH, Abdul Kadir H, Tayyab S
    ScientificWorldJournal, 2013;2013:981902.
    PMID: 24222758 DOI: 10.1155/2013/981902
    Protein stabilizing potential of honey was studied on a model protein, bovine serum albumin (BSA), using extrinsic fluorescence of fluorescein isothiocyanate (FITC) as the probe. BSA was labelled with FITC using chemical coupling, and urea and thermal denaturation studies were performed on FITC-labelled BSA (FITC-BSA) both in the absence and presence of 10% and 20% (w/v) honey using FITC fluorescence at 522 nm upon excitation at 495 nm. There was an increase in the FITC fluorescence intensity upon increasing urea concentration or temperature, suggesting protein denaturation. The results from urea and thermal denaturation studies showed increased stability of protein in the presence of honey as reflected from the shift in the transition curve along with the start point and the midpoint of the transition towards higher urea concentration/temperature. Furthermore, the increase in ΔG D (H2O) and ΔG D (25°C) in presence of honey also suggested protein stabilization.
    Matched MeSH terms: Serum Albumin/chemistry*; Serum Albumin, Bovine/chemistry*
  9. Mathavan VM, Boh BK, Tayyab S
    Indian J. Biochem. Biophys., 2009 Aug;46(4):325-31.
    PMID: 19788065
    The interaction of crythrosine B (ErB), a commonly used dye for coloring foods and drinks, with bovine scrum albumin (BSA) was investigated both in the absence and presence of bilirubin (BR) using absorption and absorption difference spectroscopy. ErB binding to BSA was reflected from a significant red shift of 11 nm in the absorption maximum of ErB (527 nm) with the change in absorbance at lamdamax. Analysis of absorption difference spectroscopic titration results of BSA with increasing concentrations of ErB3 using Benesi-Hildebrand equation gave the association constant, K as 6.9 x 10(4) M(-1). BR displacing action of ErB was revealed by a significant blue shift in the absorption maximum, accompanied by a decrease in absorbance difference at lamdamax in the difference spectrum of BR-BSA complex upon addition of increasing concentrations of ErB. This was further substantiated by fluorescence spectroscopy, as addition of increasing concentrations of ErB to BR-BSA complex caused a significant decrease in fluoresccnce at 510 nm. The results suggest that ErB binds to a site in the vicinity of BR binding site on BSA. Therefore, intake of ErB may increase the risk of hyperbilirubinemia in the healthy subjects.
    Matched MeSH terms: Serum Albumin/chemistry; Serum Albumin, Bovine/chemistry*
  10. Migasena P, Maegraith BG
    Med J Malaya, 1968 Mar;22(3):250.
    PMID: 4234388
    Matched MeSH terms: Serum Albumin, Radio-Iodinated/blood; Serum Albumin, Radio-Iodinated/cerebrospinal fluid; Serum Albumin, Radio-Iodinated/metabolism*
  11. Riley PA
    JUMMEC, 1996;1:17-19.
    The conventional use of aminoglycoside antibiotics has several disadvantages including the need for regular pre- and post-dose assaying and the risks of toxicity. Achieving a therapeutic and non-toxic serum concentration may be difficult in many patients especially those with severe sepsis. Correct timing of doses and assays is essential, but this is often difficult to achieve. Many of these difficulties may be remedied by the use of once daily dosing. This dosing schedule appears to be equally effective as the conventional method and i s also less toxic. There are many other advantages including the need for less assays and venepuncture resulting in reduced costs. KEYWORDS: Aminoglycosides, antibiotic therapy, toxicity, therapeutic monitoring
    Matched MeSH terms: Serum
  12. Al-Joudi FS
    Singapore Med J, 2005 Dec;46(12):710-3.
    PMID: 16308645
    INTRODUCTION: Decreased serum albumin (SA) levels have been used extensively as prognostic indicators in many chronic debilitating diseases. The decrease may be partly compensated by globular proteins. The failure of globulins to compensate may reflect advanced disease. We examined the prognostic value of the level of serum globulins in colorectal and breast cancers.
    METHODS: Data of 80 patients with advanced colon and breast cancers were analysed. Of these, 46 patients died within six months of measurement of their serum proteins, and the rest were followed-up for more than six months after measurements of their serum proteins were taken. A mathematical formula, representing the globulin compensation index (GCI), was recently developed from the measured SA levels and globulins. Patients were then classified into three categories: negative GCI and negative compensation; GCI of 0 to less than 1.0 with partial compensation; and GCI equal or greater than 1.0 with full compensation.
    RESULTS: Among the deceased patients, 45.7 percent had negative GCI, compared to 26.5 percent of patients in the survivors group. For partial compensation, 30.4 percent of patients were from the deceased group, and 32.4 percent were from the survivors group. For full compensation (elevated GCI), 23.9 percent of patients were from the deceased group, compared to 41.1 percent from the survivors group (p-value equals 0.031).
    CONCLUSION: Patients with low GCI are more likely to have bad prognoses, whereas those with higher GCI have more favourable prognoses. Globulin compensation may be a reliable prognostic factor in advanced colorectal and breast cancers, and possibly in other chronic illnesses. The GCI may serve as a useful tool in the measurement of this compensation.
    Matched MeSH terms: Serum Albumin/analysis*; Serum Globulins/analysis*
  13. Kong KW, Mat-Junit S, Ismail A, Aminudin N, Abdul-Aziz A
    Food Chem, 2014 Mar 1;146:85-93.
    PMID: 24176317 DOI: 10.1016/j.foodchem.2013.09.012
    The polyphenolic profiles and antioxidant activities of the water extracts of Barringtonia racemosa shoots (leaves and stems) were explored. Two methods, freeze drying and air drying, for preparation of the shoots, were also compared. Freeze drying was better as air drying caused 5-41% reduction of polyphenols. Three phenolic acids and three flavonoids were identified, using UHPLC. The descending order of polyphenols in the leaves and stems was gallic acid>ellagic acid>quercetin>protocatechuic acid>rutin>kaempferol. In vitro antioxidant analyses were performed using biological samples. In the LDL oxidation assay, B. racemosa leaf extract (IC50=73.0μg/ml) was better than stem extract (IC50=226μg/ml) at inhibiting the formation of TBARS and lipid hydroperoxides. Similar trends were observed for serum and haemoglobin oxidation. B. racemosa leaf extract was better than its stem extract in delaying the time required to oxidise haemoglobin to methaemoglobin. The high polyphenolic content of B. racemosa shoots could have contributed towards their antioxidative effects.
    Matched MeSH terms: Serum/chemistry*
  14. Feroz SR, Mohamad SB, Bakri ZS, Malek SN, Tayyab S
    PLoS One, 2013;8(10):e76067.
    PMID: 24116089 DOI: 10.1371/journal.pone.0076067
    Interaction of a pharmacologically important flavonoid, pinostrobin (PS) with the major transport protein of human blood circulation, human serum albumin (HSA) has been examined using a multitude of spectroscopic techniques and molecular docking studies. Analysis of the fluorescence quenching data showed a moderate binding affinity (1.03 × 10(5) M(-1) at 25°C) between PS and HSA with a 1∶1 stoichiometry. Thermodynamic analysis of the binding data (ΔS = +44.06 J mol(-1) K(-1) and ΔH = -15.48 kJ mol(-1)) and molecular simulation results suggested the involvement of hydrophobic and van der Waals forces, as well as hydrogen bonding in the complex formation. Both secondary and tertiary structural perturbations in HSA were observed upon PS binding, as revealed by intrinsic, synchronous, and three-dimensional fluorescence results. Far-UV circular dichroism data revealed increased thermal stability of the protein upon complexation with PS. Competitive drug displacement results suggested the binding site of PS on HSA as Sudlow's site I, located at subdomain IIA, and was well supported by the molecular modelling data.
    Matched MeSH terms: Serum Albumin/metabolism*
  15. Low SC, Shaimi R, Thandaithabany Y, Lim JK, Ahmad AL, Ismail A
    Colloids Surf B Biointerfaces, 2013 Oct 1;110:248-53.
    PMID: 23732801 DOI: 10.1016/j.colsurfb.2013.05.001
    Protein adsorption onto membrane surfaces is important in fields related to separation science and biomedical research. This study explored the molecular interactions between protein, bovine serum albumin (BSA), and nitrocellulose films (NC) using electrokinetic phenomena and the effects of these interactions on the streaming potential measurements for different membrane pore morphologies and pH conditions. The data were used to calculate the streaming ratios of membranes-to-proteins and to compare these values to the electrostatic or hydrophobic attachment of the protein molecules onto the NC membranes. The results showed that different pH and membrane pore morphologies contributes to different protein adsorption mechanisms. The protein adsorption was significantly reduced under conditions where the membrane and protein have like-charges due to electrostatic repulsion. At the isoelectric point (IEP) of the protein, the repulsion between the BSA and the NC membrane was at the lowest; thus, the BSA could be easily attached onto the membrane/solution interface. In this case, the protein was considered to be in a compact layer without intermolecular protein repulsions.
    Matched MeSH terms: Serum Albumin, Bovine/chemistry*
  16. Nang CF, Osman K, Budin SB, Ismail MI, Jaffar FH, Mohamad SF, et al.
    Andrologia, 2012 May;44 Suppl 1:447-53.
    PMID: 21806660 DOI: 10.1111/j.1439-0272.2011.01203.x
    Liquid nitrogen preservation in remote farms is a limitation. The goal of this study was to determine optimum temperature above freezing point for bovine spermatozoa preservation using bovine serum albumin (BSA) as a supplementation. Pooled semen sample from three ejaculates was subjected to various BSA concentration (1, 4, 8 and 12 mg ml(-1)), before incubation in different above freezing point temperatures (4, 25 and 37 °C). Viability assessment was carried out against time from day 0 (fresh sample) until all spermatozoa become nonviable. Optimal condition for bovine spermatozoa storage was at 4 °C with 1 mg ml(-1) BSA for almost 7 days. BSA improved bovine spermatozoa viability declining rate to 44.28% at day 4 and 57.59% at day 7 compared to control, with 80.54% and 98.57% at day 4 and 7 respectively. Increase in BSA concentration did not improve sperm viability. Our results also confirmed that there was a strong negative correlation between media osmolarity and bovine spermatozoa survival rate with r = 0.885, P < 0.0001. Bovine serum albumin helps to improve survival rate of bovine spermatozoa stored above freezing point.
    Matched MeSH terms: Serum Albumin, Bovine/physiology*
  17. Huang XD, Liang JB, Tan HY, Yahya R, Long R, Ho YW
    J Agric Food Chem, 2011 Oct 12;59(19):10677-82.
    PMID: 21899359 DOI: 10.1021/jf201925g
    Depending on their source, concentration, chemical structure, and molecular weight, condensed tannins (CTs) form insoluble complexes with protein, which could lead to ruminal bypass protein, benefiting animal production. In this study, CTs from Leuceana leucocephala hybrid were fractionated into five fractions by a size exclusion chromatography procedure. The molecular weights of the CT fractions were determined using Q-TOF LC-MS, and the protein-binding affinities of the respective CT fractions were determined using a protein precipitation assay with bovine serum albumin (BSA) as the standard protein. The calculated number-average molecular weights (M(n)) were 1348.6, 857.1, 730.1, 726.0, and 497.1, and b values (the b value represents the CT quantity that is needed to bind half of the maximum precipitable BSA) of the different molecular weight fractions were 0.381, 0.510, 0.580, 0.636, and 0.780 for fractions 1, 2, 3, 4, and 5, respectively. The results indicated that, in general, CTs of higher molecular weight fractions have stronger protein-binding affinity than those of lower molecular weights. However, the number of hydroxyl units within the structure of CT polymers also affects the protein-binding affinity.
    Matched MeSH terms: Serum Albumin, Bovine/metabolism
  18. Halim AA, Kadir HA, Tayyab S
    J. Biochem., 2008 Jul;144(1):33-8.
    PMID: 18344543 DOI: 10.1093/jb/mvn036
    Urea and guanidine hydrochloride (GdnHCl) denaturation of bovine serum albumin (BSA) were investigated using bromophenol blue (BPB) binding as a probe. Addition of BPB to BSA produced an absorption difference spectrum in the wavelength range, 525-675 nm with a minimum at 587 nm and a maximum at 619 nm. The magnitude of absorption difference (DeltaAbs.) at 619 nm decreased on increasing urea/GdnHCl concentration and followed the denaturation curve. The denaturation was found to be a two-state, single-step transition. The transitions started at 1.75 and 0.875 M and completed at 6.5 and 3.25 M with the mid point occurring around 4.0 and 1.5 M urea and GdnHCl concentrations, respectively. The value of free energy of stabilization, DeltaGDH2O as determined from urea and GdnHCl denaturation curves was found to be 4041 and 4602 cal/mol, respectively. Taken together, these results suggest that BPB binding can be used as a probe to study urea and GdnHCl denaturation of BSA.
    Matched MeSH terms: Serum Albumin, Bovine/chemistry*
  19. Faizul FM, Abdul Kadir H, Tayyab S
    J. Photochem. Photobiol. B, Biol., 2008 Jan 30;90(1):1-7.
    PMID: 18024146
    The interaction between bromocresol purple (BCP) and bovine serum albumin (BSA)/porcine serum albumin (PSA) was investigated both in the absence and presence of bilirubin (BR) using absorption/absorption difference spectroscopy. A significant red shift in the absorption maxima of BCP accompanied by a decrease in absorbance was indicative of BCP binding to albumin. The titration of BSA and PSA with BCP using absorption difference spectroscopy and analysis of results by Benesi-Hildebrand equation yielded the values of association constant, K as 9.9+/-0.9x10(4)Lmol(-1) and 4.1+/-0.3x10(4)Lmol(-1) for BSA and PSA, respectively. The differential extinction coefficient (Deltaepsilon) of 34,484M(-1)cm(-1) at 615nm and 41,870M(-1)cm(-1) at 619nm were estimated for BSA and PSA, respectively. Decrease in (DeltaAbs.)(615nm) of BCP-BSA complex with the increase in ionic strength suggested the role of hydrophobic interactions in the binding phenomenon. A significant blue shift in the absorption maxima and change in (DeltaAbs)(lambdamax) values of BR-albumin complexes upon addition of increasing concentrations of BCP revealed the BR displacing action of BCP on albumin molecule.
    Matched MeSH terms: Serum Albumin/chemistry*
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