Topic
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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TL;DR: It was found that female mice developed a stronger and longer lasting immune response and thatfemale mice were more responsive to small doses of antigen.
Abstract: SummaryThe immune response to a protein antigen (BSA, bovine serum albumin) was compared in male and female mice. It was found that female mice developed a stronger and longer lasting immune response and that female mice were more responsive to small doses of antigen. An explanation based on the effect estrogens have on phagocytosis is discussed.
125 citations
TL;DR: It is possible that the frequent identification of cellular actin in a number of enveloped viruses may be attributed to the interaction of actin and M protein or its equivalent.
Abstract: Evidence for an interaction of the membrane (M) protein of Newcastle disease and Sendai viruses with cellular actin was obtained by three different techniques. M protein linked to Sepharose 4B was found to bind actin, but not myoglobin or bovine serum albumin, and to selectively remove actin from a mixture of these three proteins. Sedimentation of a mixture of M protein and F-actin through a sucrose gradient resulted in sedimentation of M protein with actin. Control proteins, bovine serum albumin and cytochrome c, did not sediment with actin. In circular dichroism studies, M protein added to actin in a 1:1 complex resulted in a significant increase in negative ellipticity at 220 nm, which corresponds to an increase in alpha-helix and a decrease in beta-structure and random coil. This is indicative of an interaction between M protein and actin. It is possible that the frequent identification of cellular actin in a number of enveloped viruses may be attributed to the interaction of actin and M protein or its equivalent.
125 citations
TL;DR: A radioimmunoassay has been developed for the detection and quantification of a human serum polypeptide that has growth-promoting activity for confluent Balb/c-3T3 cells, demonstrating that the antigenic determinants of the growth factor have a degree of species specificity.
Abstract: A radioimmunoassay has been developed for the detection and quantification of a human serum polypeptide that has growth-promoting activity for confluent Balb/c-3T3 cells. Antiserum to this growth factor does not recognize antigens in mouse, guinea pig, or bovine serum but does detect some crossreacting antigen in the serum of the New World monkey Cebus albifrons and more in the serum of the Old World rhesus monkeys Macaca mulatta and M. fascicularis, demonstrating that the antigenic determinants of the growth factor have a degree of species specificity. Serum derived from whole human blood contains approximately 770 pg of the growth factor per mg of protein; serum derived from platelet-poor blood contains about 112 pg of the growth factor per mg of protein. As much as 1 microng of the growth factor per mg of protein has been recovered from human platelets by heating them at 100 degrees for 2 min. Approximately 1-2 ng of the growth factor, in either whole serum or platelets, stimulates 5 to 10 X 10(3) confluent Balb/c-3T3 cells to replicate. The heat treatment of platelets allows the purification and quantitative recovery of the growth factor from blood.
125 citations
TL;DR: X-ray fiber diffraction patterns of denatured bovine serum albumin suggested that the protein had a similar cross-beta structure to that of amyloid fibrils, which is consistent with the aggregates seen during food processing, being amyloids-like in nature.
Abstract: Protein aggregation is important in food processing, and this work investigated the aggregation of food proteins as a source of amyloid fibrils for use in bionanotechnology. Both purified and crude mixtures of albumin proteins were denatured by heat, which caused aggregation to occur. Protein denaturation was measured by using circular dichroism spectrometry and by following thioflavin T fluorescence, which is widely used as a diagnostic test for amyloid formation. There was a good correlation between the increase in thioflavin T fluorescence and loss of helical structure as the temperature was increased. Formation of thioflavin T fluorescence was dependent on temperature, but less dependent on salt and protein concentration. X-ray fiber diffraction patterns of denatured bovine serum albumin suggested that the protein had a similar cross-β structure to that of amyloid fibrils. These results are consistent with the aggregates seen during food processing, being amyloid-like in nature. Keywords: Ovalbumin; b...
124 citations
TL;DR: The organic precipitants decreased (P < 0.05) free amino acid concentrations in a protein concentration dependent manner while the acid precipitant had no effect.
Abstract: The effect of the protein precipitants acetone, acetonitrile, perchloric acid and trichloroacetic acid on free amino acid concentrations in supernatants from ovine plasma and bovine serum albumin s...
124 citations