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Bovine serum albumin

About: Bovine serum albumin is a research topic. Over the lifetime, 19981 publications have been published within this topic receiving 571291 citations. The topic is also known as: BSA.


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Journal ArticleDOI
TL;DR: The purification of another form of inositolphospholipid-specific phospholipase C from bovine brain cytosol is reported, and the comparison of the catalytic properties of the three isozymes are compared.
Abstract: We previously reported that cytosolic fractions of bovine brain contain two immunologically distinct forms of phospholipase C (PLC), PLC-I and PLC-II. We now report the purification of another form of inositolphospholipid-specific phospholipase C from bovine brain cytosol, designated PLC-III, and the comparison of the catalytic properties of the three isozymes. Approximately 450 micrograms of pure PLC-III was obtained from 36 bovine brains, and it had a final specific activity of 30-40 mumol of phosphatidylinositol hydrolyzed per min per mg of enzyme in the presence of 0.1% deoxycholate. PLC-III exhibited an apparent Mr of 85,000 in NaDodSO4/PAGE, which is considerably smaller than the Mr of 150,000 for PLC-I and 145,000 for PLC-II. Neither of the two mixtures of monoclonal antibodies nor the rabbit polyclonal antibodies directed against either PLC-I or PLC-II cross-reacted with PLC-III. The catalytic properties of the three isozymes were studied by using small unilamellar vesicles prepared from either phosphatidylinositol (PtdIns) or phosphatidylinositol 4,5-bisphosphate (PtdInsP2) as substrates. Hydrolysis of both PtdIns and PtdInsP2 by the three enzymes was dependent on Ca2+. However, at low Ca2+ concentration, PtdInsP2 was the preferred substrate for all three enzymes. When PtdIns was the substrate, the three enzymes exhibited similar specific activities at their optimum pH, which was 4.8 for PLC-I, 5.0 for PLC-II, and 5.5 for PLC-III. But at neutral pH, the order of specific activity was PLC-III greater than PLC-II greater than PLC-I. In contrast, the order of specific activity was PLC-I greater than PLC-III greater than PLC-II for PtdInsP2 hydrolysis, which means that PLC-I is the most specific for PtdInsP2. The three enzymes were affected differently by bovine serum albumin: inhibition of PLC-I and activation of PLC-III were observed, whereas PLC-II was unaffected. This observation suggests that any putative protein effectors for PLC should be critically scrutinized.

199 citations

Journal ArticleDOI
TL;DR: Although IgG1 is selectively concentrated by the bovine mammary tissue, no selectivity has been demonstrated for the highly permeable calf's gut, and the reason for the failure of some calves to absorb colostral immunoglobulins is unknown, additional research endeavors into the distribution, genetics, function, and synthesis of thebovine Immunoglobulin are most needed.

199 citations

Journal ArticleDOI
TL;DR: Spectral and titrimetric data are reported which suggest that the Cu(II)-binding site for both albumin and peptide is a chelate locus involving multiple nitrogenous ligands in the neutral pH range, and that a histidyl residue occupies position 3 in the peptide chain.

199 citations

Journal ArticleDOI
09 Apr 2004-Langmuir
TL;DR: The results point to a weak attractive interaction between PEO and protein, with protein repellency of a densely PEO-brushed surface ascribed to a high activation energy for the protein molecules to enter the brush.
Abstract: Solid surfaces are modified by grafting poly(ethylene oxide), PEO, to influence their interaction with indwelling particles, in particular molecules of bovine serum albumin and human plasma proteins. As a rule, the grafted PEO layers suppress protein adsorption. The suppression is most effective when the PEO layer is in a molecular brush conformation having a reciprocal grafting density (area per grafted PEO chain) less than the dimensions of the protein molecules. Nevertheless, the protein molecules may penetrate the PEO brush to some extent. For a given grafting density, the penetration is facilitated by increasing thickness of the brush. Tenuous brushes of reciprocal grafting densities exceeding the protein molecular dimensions enhance protein adsorption. The results point to a weak attractive interaction between PEO and protein. The protein repellency of a densely PEO-brushed surface is ascribed to a high activation energy for the protein molecules to enter the brush. Varying the temperature between 2...

199 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023475
2022983
2021423
2020460
2019468
2018489