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: Peroxynitrite is able to oxidize a protein, bovine serum albumin (BSA), to the corresponding protein‐thiyl free radical as demonstrated by electron paramagnetic resonance (EPR)‐spin‐trapping experiments with both α‐phenyl‐N‐tert‐butyl nitrone (PBN) and 5,5‐dimethyl‐1 ‐pyrroline‐ N‐oxide (DMPO).
138 citations
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TL;DR: A new poly(ethylene glycol)-based copolymer containing multiple thiol (-SH) groups was cross-linked in situ to form a polymer hydrogel under mild conditions, making it particularly useful for delivery of fragile therapeutics, such as proteins.
138 citations
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TL;DR: It is shown that the simple diffusion theory is inadequate to explain quantitatively the kinetics of protein adsorption, and specific, conformation-dependent, solute-solvent and solutes-interface interactions also seem to influence the kinetic of adsor adaptation of proteins.
138 citations
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TL;DR: Results indicated that the surface modification by blending citric acid grafted polyurethane provided practical application of the membranes with good biocompatibility, especially the anticoagulant property; and the membranes could be used in blood purification fields, such as hemodialysis and bioaritificial liver assist devices.
138 citations
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TL;DR: Data indicate that serine-dependent proteases hae a critical role in triggering and/or effecting cell-mediated cytolysis, and it seems likely that several of the plasma antiproteases, including alpha 1 antitrypsin and alpha 1 antichymotryps in, are capable of influencing natural cytotoxicity.
Abstract: Human natural cell-mediated cytotoxicity is inhibited by macromolecular protease inhibitors. Human plasma alpha 1 antiproteases are more effective than the plant antiproteases lima bean trypsin inhibitor and soybean trypsin inhibitor for reduction of cytotoxicity to the "slow" targets T24 human bladder carcinoma and NKI-1 melanoma. This inhibition of natural cytotoxicity is more readily demonstrable in serum-free medium containing crystalline bovine serum albumin than in medium containing fetal calf serum. Although electrophoretically homogeneous plasma alpha 1 antitrypsin inhibits natural cytotoxicity, partially purified alpha 1 antitrypsin preparations that contain several apha 1 proteins are more inhibitory at equivalent trypsin inhibitory capacities. Partially purified alpha 1 antichymotrypsin with no antitrypsin activity is an extremely potent inhibitor. Thus, it seems likely that several of the plasma antiproteases, including alpha 1 antitrypsin and alpha 1 antichymotrypsin, are capable of influencing natural cytotoxicity. These data indicate that serine-dependent proteases hae a critical role in triggering and/or effecting cell-mediated cytolysis. Furthermore, since alpha 1 antichymotrypsin and alpha 1 antitrypsin are acute phase proteins, the increase in plasma concentration or turnover rates of the proteins could influence natural killer cell activity in vivo.
137 citations