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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.


Papers
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Journal ArticleDOI
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

Journal ArticleDOI
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

Journal ArticleDOI
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

Journal ArticleDOI
Lulu Li1, Chong Cheng1, Tao Xiang1, Min Tang1, Weifeng Zhao1, Shudong Sun1, Changsheng Zhao1 
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

Journal Article
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


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