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: The heme-binding protein of rabbit serum (H BP-93) proved to be unusually sensitive and the partial protection of HBP-93 to degradation by catalase, superoxide dismutase, mannitol, and thiourea suggest the involvement of reduced oxygen species in the reaction.
168 citations
TL;DR: In this article, it was shown that the thermodynamic parameters of heat-induced unfolding, measured by differential scanning calorimetry, are closely related to the prevailing chemical conditions such as pH, concentration of ions, protein purity, and protein concentration.
Abstract: Heat-treatment is one of the most commonly used processes in food preparation technology. An understanding of the thermodynamics of protein stability and of conformational changes of proteins, acquired through the measurement of the denaturation temperature, is therefore of particular importance. This paper attempts to shed light on the interpretation of recent calorimetric data on the thermal denaturation of bovine beta-lactoglobulin, alpha-lactalbumin, and bovine serum albumin by showing that thermodynamic parameters of heat-induced unfolding, measured by differential scanning calorimetry, are closely related to the prevailing chemical conditions such as pH, concentration of ions, protein purity, and protein concentration.
168 citations
Journal Article•
TL;DR: In a number of tissues of C3H mice after administration of [14C]misonidazole, radioactivity was detected in the DNA, RNA, and protein fractions and it is postulated that nit mirroreduction and binding of the nitroreduction products to macromolecules is a probable mechanism for the mutagenic and cytotoxic properties of misonidrazole.
Abstract: Reduction of the nitro group occurred when [14C]misonidazole was treated with zinc dust in aqueous solution in the presence of ammonium chloride. When the reduction mixture was allowed to react with calf thymus DNA or bovine albumin, radioactivity was bound to both DNA and protein. Under the same conditions, misonidazole did not bind to these macromolecules. Analysis of the reduction mixture indicated that the hydroxylamine, amine, and hydrazo derivatives of mizonidazole were the major products. In a number of tissues of C3H mice after administration of [14C]misonidazole, radioactivity was detected in the DNA, RNA, and protein fractions. Similar results were also obtained with Chinese hamster ovary cells incubated with the drug in the absence of oxygen. It is postulated that nitroreduction and binding of the nitroreduction products to macromolecules is a probable mechanism for the mutagenic and cytotoxic properties of misonidazole.
168 citations
TL;DR: The two techniques applied in the present study -- micro-DSC and FTIR spectroscopy -- can be concluded to provide complementary information on adsorption-induced structural changes on both the molecular and sub-molecular level (secondary structure).
167 citations
TL;DR: A significant role of phospholipid in the structural and functional properties of the receptor was suggested by the reduced binding activity observed after treatment of particulate and soluble receptors withospholipase A, and by the aggregation which occurred after exposure of the soluble receptors to phospholIPase C.
167 citations