Displaying publications 1 - 20 of 142 in total

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  1. A note of caution on the use of crystalline bovine albumin as a reference standard in the estimation of serum proteins
    De Witt GF
    Med J Malaya, 1965 Jun;19(4):303-5.
    PMID: 4220856
    Matched MeSH terms: Serum Albumin, Bovine*
  2. Characterization of bovine serum albumin partitioning behaviors in polymer-salt aqueous two-phase systems
    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*
  3. Factor affecting on the movement of protein across the blood: brain: C.S.F. barriers in Plasmodium knowlesi infected Macaca mulatta
    Migasena P, Maegraith BG
    Med J Malaya, 1968 Mar;22(3):251.
    PMID: 4234389
    Matched MeSH terms: Serum Albumin/metabolism*; Serum Albumin, Radio-Iodinated
  4. Fulltext The utilization of an index for serum globulin compensation in diseases associated with decreased serum albumin
    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*
  5. Adsorption of Bovine Serum Albumin (BSA) at the Oil/Water Interface: A Neutron Reflection Study
    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*
  6. 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*
  7. Characterization of erythrosine B binding to bovine serum albumin and bilirubin displacement
    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*
  8. The movement of radioactive albumin (I131 R.H.S.A.) from blood into C.S.F. and vice versa by dilution method in normal and Plasmodium knowlesi infected Macaca mulatta
    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*
  9. Electrophoretic interactions between nitrocellulose membranes and proteins: Biointerface analysis and protein adhesion properties
    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*
  10. Bovine serum albumin: survival and osmolarity effect in bovine spermatozoa stored above freezing point
    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*
  11. Protein-binding affinity of leucaena condensed tannins of differing molecular weights
    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
  12. Bromophenol blue binding as a probe to study urea and guanidine hydrochloride denaturation of bovine serum albumin
    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*
  13. Spectroscopic studies on the binding of bromocresol purple to different serum albumins and its bilirubin displacing action
    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*
  14. 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
  15. A practical scheme for the estimation of serum total protein and albumin
    Kua See Lai, Chew Yin La, De Witt GF, Buttery JE
    Med J Malaysia, 1973 Dec;28(2):115-7.
    PMID: 4276227
    Matched MeSH terms: Serum Albumin/analysis*
  16. Antifouling polyethersulfone hemodialysis membranes incorporated with poly (citric acid) polymerized multi-walled carbon nanotubes
    Abidin MNZ, Goh PS, Ismail AF, Othman MHD, Hasbullah H, Said N, et al.
    Mater Sci Eng C Mater Biol Appl, 2016 Nov 01;68:540-550.
    PMID: 27524052 DOI: 10.1016/j.msec.2016.06.039
    Poly (citric acid)-grafted-MWCNT (PCA-g-MWCNT) was incorporated as nanofiller in polyethersulfone (PES) to produce hemodialysis mixed matrix membrane (MMM). Citric acid monohydrate was polymerized onto the surface of MWCNTs by polycondensation. Neat PES membrane and PES/MWCNTs MMMs were fabricated by dry-wet spinning technique. The membranes were characterized in terms of morphology, pure water flux (PWF) and bovine serum albumin (BSA) protein rejection. The grafting yield of PCA onto MWCNTs was calculated as 149.2%. The decrease of contact angle from 77.56° to 56.06° for PES/PCA-g-MWCNTs membrane indicated the increase in surface hydrophilicity, which rendered positive impacts on the PWF and BSA rejection of the membrane. The PWF increased from 15.8Lm(-2)h(-1) to 95.36Lm(-2)h(-1) upon the incorporation of PCA-g-MWCNTs due to the attachment of abundant hydrophilic groups that present on the MWCNTs, which have improved the affinity of membrane towards the water molecules. For protein rejection, the PES/PCA-g-MWCNTs MMM rejected 95.2% of BSA whereas neat PES membrane demonstrated protein rejection of 90.2%. Compared to commercial PES hemodialysis membrane, the PES/PCA-g-MWCNTs MMMs showed less flux decline behavior and better PWF recovery ratio, suggesting that the membrane antifouling performance was improved. The incorporation of PCA-g-MWCNTs enhanced the separation features and antifouling capabilities of the PES membrane for hemodialysis application.
    Matched MeSH terms: Serum Albumin, Bovine/chemistry
  17. Evaluation of pendimethalin binding to human serum albumin: Insights from spectroscopic and molecular modeling approach
    Lee WQ, Affandi IS, Feroz SR, Mohamad SB, Tayyab S
    J Biochem Mol Toxicol, 2017 Feb;31(2).
    PMID: 27636401 DOI: 10.1002/jbt.21839
    Interaction of pendimethalin (PM) herbicide with the major transporter in human circulation, human serum albumin (HSA), was studied using fluorescence, circular dichroism (CD), and molecular modeling methods. The attenuation of the fluorescence intensity of HSA in the presence of PM revealed formation of the PM-HSA complex. Analysis of the fluorescence quenching data showed moderately strong binding affinity between PM and HSA. Both hydrophobic interactions and hydrogen bonding were suggested to stabilize the PM-HSA complex, based on thermodynamic data. Binding of PM to HSA induced perturbation in the microenvironment around the aromatic fluorophores as well as secondary and tertiary structural changes in the protein. Complexation of PM with HSA led to an increase in its thermal stability. Both site marker displacement and molecular modeling results suggested site I, located in subdomain IIA as the preferred binding site of PM on HSA.
    Matched MeSH terms: Serum Albumin/metabolism*
  18. The movement of fluorescent isothiocyanate (F.I.T.C.) labelled human albumin from blood into brain tissue examined by fluorescent technique in normal and Plasmodium knowlesi infected Macaca mulatta
    Migasena P, Maegraith BG
    Med J Malaya, 1968 Mar;22(3):251.
    PMID: 4234390
    Matched MeSH terms: Serum Albumin/metabolism*
  19. 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*
  20. Effect of Solution Properties and Operating Parameters on Needleless Electrospinning of Poly(Ethylene Oxide) Nanofibers Loaded with Bovine Serum Albumin
    Ramakrishnan R, Gimbun J, Ramakrishnan P, Ranganathan B, Reddy SMM, Shanmugam G
    Curr Drug Deliv, 2019;16(10):913-922.
    PMID: 31663478 DOI: 10.2174/1567201816666191029122445
    BACKGROUND: This paper presents the effect of solution properties and operating parameters of polyethylene oxide (PEO) based nanofiber using a wire electrode-based needleless electrospinning.

    METHODS: The feed solution was prepared using a PEO dissolved in water or a water-ethanol mixture. The PEO solution is blended with Bovine Serum Albumin protein (BSA) as a model drug to study the effect of the electrospinning process on the stability of the loaded protein. The polymer solution properties such as viscosity, surface tension, and conductivity were controlled by adjusting the solvent and salt content. The morphology and fiber size distribution of the nanofiber was analyzed using scanning electron microscopy.

    RESULTS: The results show that the issue of a beaded nanofiber can be eliminated either by increasing the solution viscosity or by the addition of salt and ethanol to the PEO-water system. The addition of salt and solvent produced a high frequency of smaller fiber diameter ranging from 100 to 150 nm. The encapsulation of BSA in PEO nanofiber was characterized by three different spectroscopy techniques (i.e. circular dichroism, Fourier transform infrared, and fluorescence) and the results showed the BSA is well encapsulated in the PEO matrix with no changes in the protein structure.

    CONCLUSION: This work may serve as a useful guide for a drug delivery industry to process a nanofiber at a large and continuous scale with a blend of drugs in nanofiber using a wire electrode electrospinning.

    Matched MeSH terms: Serum Albumin, Bovine/chemistry*
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