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 ability of the mature small intestine to absorb intact protein was studied in adult rats prepared with duodenal cannulas, mesenteric lymph fistulae, and portal vein cannulas to provide additional evidence for the concept that intact protein can traverse the mature intestinal epithelium under physiologic conditions.
175 citations
TL;DR: In this paper, bovine serum albumin (BSA) nanoparticles were prepared using a modified desolvation method and the surface-area-to-volume-ratio was calculated.
174 citations
TL;DR: It is reported that aspirin acetylates a variety of body constituents in vitro, including HSA, serum albumin, and other biological materials.
Abstract: HUMAN serum albumin (HSA) is permanently altered after exposure to therapeutic concentrations of acetylsalicylic acid (ASA, aspirin) either in vitro or in vivo1–3. Recently we showed that this structural alteration was the result of the acetylation of the HSA molecule by aspirin4,5. Because the acetylation of HSA by aspirin could occur by aminolysis resulting in an N-acetyl-HSA derivative, we decided to determine whether aspirin could acetylate other biological materials. We now report that aspirin acetylates a variety of body constituents in vitro.
174 citations
TL;DR: The coacervation yield for individual proteins and the degree of separation, for selected protein pairs, were studied as a function of polymer molecular weight, ionic strength, and pH.
Abstract: Selective phase separation with polyelectrolytes can be used to separate a mixture of proteins. The efficiency of separation was examined using the cationic polyelectrolyte poly(diallyldimethylammonium chloride) and the model proteins bovine serum albumin, β-lactoglobulin, γ-globulin, and ribonuclease A. The coacervation yield for individual proteins and the degree of separation, for selected protein pairs, were studied as a function of polymer molecular weight, ionic strength, and pH.
172 citations
172 citations