Displaying publications 1 - 20 of 142 in total

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  1. Attenuated Total Reflection Fourier Transform Infrared (ATR FT-IR) Spectroscopy as an Analytical Method to Investigate the Secondary Structure of a Model Protein Embedded in Solid Lipid Matrices
    Zeeshan F, Tabbassum M, Jorgensen L, Medlicott NJ
    Appl Spectrosc, 2018 Feb;72(2):268-279.
    PMID: 29022355 DOI: 10.1177/0003702817739908
    Protein drugs may encounter conformational perturbations during the formulation processing of lipid-based solid dosage forms. In aqueous protein solutions, attenuated total reflection Fourier transform infrared (ATR FT-IR) spectroscopy can investigate these conformational changes following the subtraction of spectral interference of solvent with protein amide I bands. However, in solid dosage forms, the possible spectral contribution of lipid carriers to protein amide I band may be an obstacle to determine conformational alterations. The objective of this study was to develop an ATR FT-IR spectroscopic method for the analysis of protein secondary structure embedded in solid lipid matrices. Bovine serum albumin (BSA) was chosen as a model protein, while Precirol AT05 (glycerol palmitostearate, melting point 58 ℃) was employed as the model lipid matrix. Bovine serum albumin was incorporated into lipid using physical mixing, melting and mixing, or wet granulation mixing methods. Attenuated total reflection FT-IR spectroscopy and size exclusion chromatography (SEC) were performed for the analysis of BSA secondary structure and its dissolution in aqueous media, respectively. The results showed significant interference of Precirol ATO5 with BSA amide I band which was subtracted up to 90% w/w lipid content to analyze BSA secondary structure. In addition, ATR FT-IR spectroscopy also detected thermally denatured BSA solid alone and in the presence of lipid matrix indicating its suitability for the detection of denatured protein solids in lipid matrices. Despite being in the solid state, conformational changes occurred to BSA upon incorporation into solid lipid matrices. However, the extent of these conformational alterations was found to be dependent on the mixing method employed as indicated by area overlap calculations. For instance, the melting and mixing method imparted negligible effect on BSA secondary structure, whereas the wet granulation mixing method promoted more changes. Size exclusion chromatography analysis depicted the complete dissolution of BSA in the aqueous media employed in the wet granulation method. In conclusion, an ATR FT-IR spectroscopic method was successfully developed to investigate BSA secondary structure in solid lipid matrices following the subtraction of lipid spectral interference. The ATR FT-IR spectroscopy could further be applied to investigate the secondary structure perturbations of therapeutic proteins during their formulation development.
    Matched MeSH terms: Serum Albumin, Bovine/analysis; Serum Albumin, Bovine/chemistry
  2. Mature Erythrocyte Surface Antigen Protein Identified in the Serum of Plasmodium falciparum-Infected Patients
    Zainudin NS, Othman N, Muhi J, Abdu Sani AA, Noordin R
    Am J Trop Med Hyg, 2015 Dec;93(6):1268-73.
    PMID: 26392156 DOI: 10.4269/ajtmh.15-0333
    This study was performed to identify circulating Plasmodium falciparum proteins in patient serum, which may be useful as diagnostic markers. Depletion of highly abundant proteins from each pooled serum sample obtained from P. falciparum-infected patients and healthy individuals was performed using the Proteoseek Antibody-Based Albumin/IgG Removal Kit (Thermo Scientific, Rockford, IL). In analysis 1, the depleted serum was analyzed directly by NanoLC-MS/MS. In analysis 2, the depleted serum was separated by two-dimensional electrophoresis followed by western blot analysis. Subsequently, the selected band was analyzed by NanoLC-MS/MS. The result of analysis 1 revealed the presence of two mature erythrocyte surface antigen (MESA) proteins and chloroquine resistance transporter protein (PfCRT). In addition, analysis 2 revealed an antigenic 75-kDa band when the membrane was probed with purified IgG from the pooled serum obtained from P. falciparum-infected patients. MS/MS analysis of this protein band revealed fragments of P. falciparum MESA proteins. Thus, in this study, two different analyses revealed the presence of Plasmodium MESA protein in pooled serum from malaria patients; thus, this protein should be further investigated to determine its usefulness as a diagnostic marker.
    Matched MeSH terms: Serum Albumin/analysis
  3. Fulltext The comparison of QT dispersion and 24 hour ambulatory blood pressure monitoring amongst diabetic patients with and without microalbuminuria
    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*
  4. Precipitation of Hevea brasiliensis latex proteins with trichloroacetic acid and phosphotungstic acid in preparation for the Lowry protein assay
    Yeang HY, Yusof F, Abdullah L
    Anal Biochem, 1995 Mar 20;226(1):35-43.
    PMID: 7785777
    Many proteins derived from the latex of Hevea brasiliensis that remain soluble in trichloroacetic acid (TCA) can be precipitated by phosphotungstic acid (PTA). A combination of 5% TCA and 0.2% PTA precipitates a wide range of proteins effectively even when they are present in low concentrations (below 1 microgram ml-1). In addition to its protein purification function, acid precipitation also increases the sensitivity of the subsequent protein assay by allowing the test sample to be concentrated. Another advantage of protein precipitation by TCA and PTA is that very small amounts of protein (of the order of 10 micrograms) can be repeatably recovered without the use of precipitate-bulking agents such as sodium deoxycholate. This general procedure of protein purification and concentration is simple and rapid, but the use of PTA may not be fully compatible with the Bradford protein assay. A modified Lowry microassay is described which enables about 3 micrograms ml-1 to be quantitated at the photometric absorbance of 0.05. When used in conjunction with protein concentration by precipitating with TCA/PTA, approximately 0.4 microgram ml-1 protein present in 6 ml of solution can be assayed.
    Matched MeSH terms: Serum Albumin, Bovine/analysis
  5. Prealbumin rather than albumin is a more sensitive indicator of acute liver disease
    Yasmin MY, Aziz B, Nazim M, Madhavan RK
    Malays J Pathol, 1993 Dec;15(2):147-50.
    PMID: 8065177
    The changes in serum prealbumin (transthyretin) and serum albumin in acute and chronic liver diseases were investigated. Albumin has long been used as a useful indicator of liver function but serum prealbumin has recently been noted for its clinical significance in acute liver diseases. Serum prealbumin concentrations and liver function tests (albumin, bilirubin, alanine aminotransferase) were determined on blood obtained from normal donors (n = 148) and from patients suffering from liver diseases (n = 78) such as acute viral hepatitis, chronic active hepatitis, cirrhosis and hepatoma. The mean serum prealbumin concentration in normal subjects was 29.6 +/- 4.82 mg/dl while the mean serum prealbumin concentration in patients with liver disease was greatly reduced (acute viral hepatitis = 15.3 +/- 7.4mg/dl; chronic active hepatitis = 10.2 +/- 6.6mg/dl; cirrhosis = 9.9 +/- 6.4mg/dl and hepatoma = 10.7 +/- 4.2). Albumin concentrations dropped slightly (13% compared to control) in acute viral hepatitis but dropped markedly (28% compared to control) in chronic liver diseases. The study suggests that serum prealbumin concentration might be a more sensitive indicator than albumin in assessing liver dysfunction in acute liver diseases.
    Matched MeSH terms: Serum Albumin/analysis*
  6. Preparation and Characterization of Alginate Microparticles Containing a Model Protein for Oral Administration in Gnotobiotic European Sea Bass (Dicentrarchus labrax) Larvae
    Yaacob EN, Goethals J, Bajek A, Dierckens K, Bossier P, De Geest BG, et al.
    Mar Biotechnol (NY), 2017 Aug;19(4):391-400.
    PMID: 28643227 DOI: 10.1007/s10126-017-9758-4
    Aquaculture is the fastest growing animal production sector. However, the production of marine fish is still hampered by the high mortality rate in the first few weeks after hatching. Mortality in larvae is often caused by microbial infections. Today, the incorporation of immunostimulants into microparticles provides us new tools to enhance disease resistance in marine larviculture. In this study, we prepared alginate microparticles loaded with the model antigen fluorescein isothiocyanate conjugated-bovine serum albumin. Optimum concentrations of alginate and CaCl2, the correct alginate viscosity and the appropriate preparatory conditions led to the creation of desirable microparticles with the correct size for oral feeding in gnotobiotic European sea bass larvae. The prepared alginate microparticles were stable in sea water and were successfully ingested by gnotobiotic sea bass larvae at day after hatching 7 without causing any negative effects. Results suggest the suitability of this drug delivery system for targeting the innate immune system of fish larvae in order to enhance disease resistance and thus reduce mortality in larviculture.
    Matched MeSH terms: Serum Albumin, Bovine
  7. Fulltext Honey-induced protein stabilization as studied by fluorescein isothiocyanate fluorescence
    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*
  8. Differential-based biosensor array for fluorescence-chemometric discrimination and the quantification of subtle chloropropanols by cross-reactive serum albumin scaffolding
    Wong SF, Low KH, Khor SM
    Talanta, 2020 Oct 01;218:121169.
    PMID: 32797922 DOI: 10.1016/j.talanta.2020.121169
    Food contamination is a serious concern because of a high level of chemicals in food causes severe health issues. Safeguarding the public from the risk of adulterated foods has become a challenging mission. Chloropropanols are of importance to food safety and food security because they are common chemical food contaminants and believed to be carcinogenic to humans. In chemical sensing, chloropropanols are challenging analytes owing to the lacking diversity of functional groups and difficulty in targeting the hydroxyl group in aqueous environments. Moreover, because of their small molecular size, the compositions of chloropropanols remain challenging for achieving chromatographic determination. Herein, to simulate human smell and taste sensations, serum albumins, which are protein-based receptors, were introduced as low-selective receptors for differential sensing. Utilizing serum albumins, a fluorophore (PRODAN), and an additive (ascorbic acid), a differential-based optical biosensor array was developed to detect and differentiate chloropropanols. By integrating the sensor array with linear discriminant analysis (LDA), four chloropropanols were effectively differentiated based on their isomerism properties and the number of the hydroxyl groups, even at ultra-low concentration (5 nM). This concentration is far below the maximum tolerable level of 0.18 μM for chloropropanols. The sensing array was then employed for chloropropanols differentiation and quantification in the complex mixtures (e.g., synthetic soy and dark soy sauces). Leave-one-out cross-validation (LOOCV) analysis demonstrated 100% accurate classification for all tests. These results signify our differential sensing array as a practical and powerful tool to speedily identify, differentiate, and even quantify chloropropanols in food matrices.
    Matched MeSH terms: Serum Albumin
  9. Serum albumin variants in three Malaysian racial groups
    Welch QB, Lie-Injo LE
    Hum. Hered., 1972;22(5):503-7.
    PMID: 4670071
    Matched MeSH terms: Serum Albumin*
  10. Synthesis of fluorescent carbon dots via simple acid hydrolysis of bovine serum albumin and its potential as sensitive sensing probe for lead (II) ions
    Wee SS, Ng YH, Ng SM
    Talanta, 2013 Nov 15;116:71-6.
    PMID: 24148375 DOI: 10.1016/j.talanta.2013.04.081
    Carbon dots have great potential to be utilised as an optical sensing probe due to its unique photoluminescence and less toxic properties. This work reports a simple and novel synthesis method of carbon dots via direct acid hydrolysis of bovine serum albumin protein in a one-pot approach. Optimisation of the important synthetic parameters has been performed which consists of temperature effect, acid to protein ratio and kinetics of reaction. Higher temperature has promoted better yield with shorter reaction time. The carbon dots obtained shows a strong emission at the wavelength of 400 nm with an optimum excitation of 305 nm. The potential of the carbon dots as optical sensing probe has been investigated on with different cations that are of environmental and health concern. The fluorescence of the carbon dots was significantly quenched particularly by lead (II) ions in a selective manner. Further analytical study has been performed to leverage the performance of the carbon dots for lead (II) ions sensing using the standard Stern-Volmer relationship. The sensing probe has a dynamic linear range up to 6.0 mM with a Stern-Volmer constant of 605.99 M(-1) and a limit of detection (LOD) of 5.05 μM. The probe performance was highly repeatable with a standard deviation below 3.0%. The probe suggested in this study demonstrates the potential of a more economical and greener approach that uses protein based carbon dots for sensing of heavy metal ions.
    Matched MeSH terms: Serum Albumin, Bovine/chemistry*
  11. Fulltext An enzyme immunoassay for advanced glycosylation end-products in serum
    Wan Nazaimoon WM, Khaid BAK
    Malays J Pathol, 1998 Dec;20(2):83-9.
    PMID: 10879267
    We successfully developed an in-house, competitive enzyme immunoassay to measure advanced glycosylation end-products (AGE) in serum. The assay involved coating microtitre wells with AGE-BSA at 8 micrograms/ml for 4 hours, followed by overnight incubation of 20 microliters sample (prediluted at 1:6) with 80 microliters antiserum (1:8000). HRP-labelled goat anti-rabbit was used as the second antibody and 3,5',5,5'-tetramethylbenzidine dihydrochloride as the substrate. Incubation was carried out at 4 degrees C. As suggested in an earlier study, we standardised the AGE units against normal human serum (NHS). Thus, one AGE unit was defined as the inhibition that resulted when the 1:6 diluted NHS was assayed. Mean (+/- SD) AGE level in normal subjects (n = 37) was significantly lower than in diabetes subjects with microalbuminuria (n = 57) (6.0 +/- 0.7 versus 10.2 +/- 4.7 units/ml, p = 0.0001). With the availability of in-house assay and by standardising the AGE unit with the other laboratories, more studies could be undertaken and results compared, and possibly, further elucidate the roles of AGE in the pathogenesis of diabetic complications.
    Matched MeSH terms: Serum Albumin, Bovine/immunology
  12. Fulltext The effects of intermittent fasting during the month of Ramadan in chronic haemodialysis patients in a tropical climate country
    Wan Md Adnan WA, Zaharan NL, Wong MH, Lim SK
    PLoS One, 2014;9(12):e114262.
    PMID: 25546434 DOI: 10.1371/journal.pone.0114262
    Chronic kidney disease is an emerging problem in the majority Muslim countries. Despite the uncertainties of the risks involved, some Muslim patients undergoing chronic haemodialysis choose to observe intermittent fasting during the month of Ramadan. This study aims to investigate the effect of Ramadan fasting in haemodialysis patients residing in a tropical climate country.
    Matched MeSH terms: Serum Albumin/analysis
  13. In silico and BSA binding study of some new biological analogs of 1,2,4-triazolependant with azinane through microwave and conventional synthesis
    Virk NA, Rehman A, Abbasi MA, Siddiqui SZ, Ashraf A, Lateef M, et al.
    Pak J Pharm Sci, 2018 Nov;31(6 (Supplementary):2645-2654.
    PMID: 30587474
    Microwave and conventional techniques were employed to synthesize a novel array of compounds 7a-g with 1,2,4-triazole and piperidine rings having great biological importance. The microwave assisted method has a better operational scope with respect to time and yield comparative to the conventional method. 1H-NMR, 13C-NMR and IR techniques were employed to justify the structure of synthesized compounds. The antioxidant, butyrylcholinesterase inhibition and urease inhibition potential of every synthesized compound was evaluated. Every member of the synthesized series was found potent against mentioned activities. Compound 7g was the most active anti-urease agent having IC50 (μM) value 16.5±0.09 even better than the thiourea with an IC50(μM) value of 24.3±0.24. The better urease inhibition potential of 7g was also elaborated and explained by docking and bovine serum albumin (BSA) binding studies.
    Matched MeSH terms: Serum Albumin, Bovine/chemical synthesis; Serum Albumin, Bovine/metabolism*
  14. Fulltext Pattern of rheumatoid arthritis in West Malaysia
    Toh BH, Sengupta S, Ang AH, White JC, Lau KS
    Ann Rheum Dis, 1973 Mar;32(2):151-6.
    PMID: 4120913 DOI: 10.1136/ard.32.2.151
    In West Malaysia RA appears to be less common than in temperate climates, but more common than in tropical Africa; furthermore, the incidence of gout and SLE is comparable. The clinical manifestations of RA are milder than those seen in more temperate climates. Subcutaneous rheumatoid nodules have not been observed. Positive serological tests for RF are significantly higher than in the general Malaysian population, but still lower than those reported for patients with RA in temperate climates. Of the three main ethnic groups, the highest incidence of positive results is found in the Chinese.
    Study site: Arthritis Clinic, University Hospital, Kuala Lumpur (University Malaya Medical Centre, UMMC, Kuala Lumpur, Malaysia)
    Matched MeSH terms: Serum Albumin
  15. Impact of bovine and human serum albumin on Curcumin in vitro activity against Staphylococcus aureus
    Teow SY, Ali SA
    Pak J Pharm Sci, 2017 May;30(3):891-895.
    PMID: 28653935
    This study evaluated the impact of pH (7.4 and 6.5), bovine serum albumin (BSA), and human serum albumin (HSA) on Curcumin activity against 2 reference, 1 clinical, and 10 environmental strains of Staphylococcus aureus (S. aureus). Minimal inhibitory concentrations (MICs) of Curcumin against S. aureus were statistically indifferent (p>0.05) at pH7.4 and pH6.5. Activity of Curcumin against S. aureus was reduced by two folds in the presence of 1.25-5% BSA/HSA.
    Matched MeSH terms: Serum Albumin/chemistry
  16. Altered antibacterial activity of Curcumin in the presence of serum albumin, plasma and whole blood
    Teow SY, Ali SA
    Pak J Pharm Sci, 2017 Mar;30(2):449-457.
    PMID: 28649069
    Antibacterial effect is one of the major therapeutic activities of plant-derived Curcumin. This work evaluated the effect of serum albumin, human plasma, and whole blood on the in vitro activity of Curcumin against eight clinical bacterial isolates by standard broth microdilution and plate-counting methods. Toxicological effects of Curcumin towards human red blood cells (RBCs) and peripheral blood mononuclear cells (PBMCs) were also investigated. Curcumin exhibited weak activity against gram-negative bacteria, except Escherichia coli and Shigella flexneri were susceptible and was most active against gram-positive bacteria: Staphylococcus aureus, Streptococcus pyogenes and Enterococcus faecalis. The antibacterial activity was impaired in the presence of bovine serum albumin (BSA), human plasma and whole blood. Curcumin was not toxic to PBMCs and RBCs at 200μg/mL. Furthermore, Curcumin showed synergistic activity in combination with antibiotics: Ciprofloxacin, Gentamicin, Vancomycin and Amikacin against Staphylococcus aureus. This study demonstrated that the interaction of Curcumin with plasma proteins diminishes its in vitro antibacterial activity. Curcumin derivatives with reduced affinity for plasma protein may improve the bioavailability and antibacterial activities.
    Matched MeSH terms: Serum Albumin/adverse effects*
  17. Exploring the interaction between the antiallergic drug, tranilast and human serum albumin: Insights from calorimetric, spectroscopic and modeling studies
    Tayyab S, Zaroog MS, Feroz SR, Mohamad SB, Malek SN
    Int J Pharm, 2015 Aug 1;491(1-2):352-8.
    PMID: 26142245 DOI: 10.1016/j.ijpharm.2015.06.042
    The interaction of tranilast (TRN), an antiallergic drug with the main drug transporter in human circulation, human serum albumin (HSA) was studied using isothermal titration calorimetry (ITC), fluorescence spectroscopy and in silico docking methods. ITC data revealed the binding constant and stoichiometry of binding as (3.21 ± 0.23) × 10(6)M(-1) and 0.80 ± 0.08, respectively, at 25°C. The values of the standard enthalpy change (ΔH°) and the standard entropy change (ΔS°) for the interaction were found as -25.2 ± 5.1 kJ mol(-1) and 46.9 ± 5.4 J mol(-1)K(-1), respectively. Both thermodynamic data and modeling results suggested the involvement of hydrogen bonding, hydrophobic and van der Waals forces in the complex formation. Three-dimensional fluorescence data of TRN-HSA complex demonstrated significant changes in the microenvironment around the protein fluorophores upon drug binding. Competitive drug displacement results as well as modeling data concluded the preferred binding site of TRN as Sudlow's site I on HSA.
    Matched MeSH terms: Serum Albumin/chemistry
  18. Binding of an anticancer drug, axitinib to human serum albumin: Fluorescence quenching and molecular docking study
    Tayyab S, Izzudin MM, Kabir MZ, Feroz SR, Tee WV, Mohamad SB, et al.
    J. Photochem. Photobiol. B, Biol., 2016 Sep;162:386-94.
    PMID: 27424099 DOI: 10.1016/j.jphotobiol.2016.06.049
    Binding characteristics of a promising anticancer drug, axitinib (AXT) to human serum albumin (HSA), the major transport protein in human blood circulation, were studied using fluorescence, UV-vis absorption and circular dichroism (CD) spectroscopy as well as molecular docking analysis. A gradual decrease in the Stern-Volmer quenching constant with increasing temperature revealed the static mode of the protein fluorescence quenching upon AXT addition, thus confirmed AXT-HSA complex formation. This was also confirmed from alteration in the UV-vis spectrum of HSA upon AXT addition. Fluorescence quenching titration results demonstrated moderately strong binding affinity between AXT and HSA based on the binding constant value (1.08±0.06×10(5)M(-1)), obtained in 10mM sodium phosphate buffer, pH7.4 at 25°C. The sign and magnitude of the enthalpy change (∆H=-8.38kJmol(-1)) as well as the entropy change (∆S=+68.21Jmol(-1)K(-1)) clearly suggested involvement of both hydrophobic interactions and hydrogen bonding in AXT-HSA complex formation. These results were well supported by molecular docking results. Three-dimensional fluorescence spectral results indicated significant microenvironmental changes around Trp and Tyr residues of HSA upon complexation with AXT. AXT binding to the protein produced significant alterations in both secondary and tertiary structures of HSA, as revealed from the far-UV and the near-UV CD spectral results. Competitive drug displacement results obtained with phenylbutazone (site I marker), ketoprofen (site II marker) and hemin (site III marker) along with molecular docking results suggested Sudlow's site I, located in subdomain IIA of HSA, as the preferred binding site of AXT.
    Matched MeSH terms: Serum Albumin/metabolism*; Serum Albumin/chemistry*
  19. Genetic studies of water buffalo blood markers. I. Red cell acid phosphatase, albumin, catalase, red cell alpha-esterase-3, group-specific component, and protease inhibitor
    Tan SG, Barker JS, Selvaraj OS, Mukherjee TK, Wong YF
    Biochem Genet, 1993 Jun;31(5-6):223-30.
    PMID: 8259925
    We have developed the methodologies for typing and family studies to establish the modes of inheritance of water buffalo red cell acid phosphatase (Acp), protease inhibitor (Pi), and group-specific component (Gc) on isoelectric focusing and albumin (Alb), red cell alpha-esterase-3 (Est-3), and catalase (Cat) on polyacrylamide gel electrophoresis. Family studies showed that Pi, Gc, Alb, and Cat are coded by autosomal genes with two codominant alleles, while Est-3 is autosomal with two codominant alleles and a recessive null allele and Acp exhibits three codominant alleles.
    Matched MeSH terms: Serum Albumin, Bovine/genetics
  20. Parametric Investigation of Batch Adsorption of Proteins onto Polymeric Particles
    Tan MX, Agyei D, Pan S, Danquah MK
    Curr Pharm Biotechnol, 2015;16(9):816-22.
    PMID: 26119365
    BACKGROUND: Effective bimolecular adsorption of proteins onto solid matrices is characterized by in-depth understanding of the biophysical features essential to optimize the adsorption performance.

    RESULTS: The adsorption of bovine serum albumin (BSA) onto anion-exchange Q-sepharose solid particulate support was investigated in batch adsorption experiments. Adsorption kinetics and isotherms were developed as a function of key industrially relevant parameters such as polymer loading, stirring speed, buffer pH, protein concentration and the state of protein dispersion (solid/aqueous) in order to optimize binding performance and adsorption capacity. Experimental results showed that the first order rate constant is higher at higher stirring speed, higher polymer loading, and under alkaline conditions, with a corresponding increase in equilibrium adsorption capacity. Increasing the stirring speed and using aqueous dispersion protein system increased the adsorption rate, but the maximum protein adsorption was unaffected. Regardless of the stirring speed, the adsorption capacity of the polymer was 2.8 mg/ml. However, doubling the polymer loading increased the adsorption capacity to 9.4 mg/ml.

    CONCLUSIONS: The result demonstrates that there exists a minimum amount of polymer loading required to achieve maximum protein adsorption capacity under specific process conditions.

    Matched MeSH terms: Serum Albumin, Bovine/chemistry
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