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: Some similarities between modifications at pH 6 and 9 are indicated and it is shown that both modifications clearly change the functional properties of globular proteins.
Abstract: BACKGROUND: The interactions between phenolic compounds and proteins can modify protein properties important in the food industry. To understand the effects of these interactions, the covalent interactions between caffeoylquinic acid (chlorogenic acid, CQA) oxidised by polyphenol oxidase (PPO) at acidic pH 6 (pH 6) and -lactalbumin, lysozyme and bovine serum albumin (BSA) were compared with non-enzymatically induced covalent interactions at alkaline pH (pH 9). The effects of these modifications on protein properties were examined. RESULTS: Both ways of modification seemed to result in protein modification mainly via dimeric rather than monomeric CQA quinones. These modifications led to a decrease in the number of free primary amino groups of the proteins. Modification with CQA alone induced a low degree of protein dimerisation, which also occurred through the action of PPO alone. Modification drastically reduced the solubility of lysozyme over a broad pH range, whereas that of -lactalbumin was strongly reduced only at pH values close to its pI. The solubility of BSA was much less affected than that of the other proteins and only at acidic pH. CONCLUSION: These results indicate some similarities between modifications at pH 6 and 9 and that both modifications clearly change the functional properties of globular proteins.
134 citations
TL;DR: The present study provides the possibility to achieve a long-term effective release of biologically active proteins from a Ca-P-coated metallic implant.
Abstract: Calcium phosphate (Ca-P) and bovine serum albumin (BSA) were coprecipitated as a coating on commercially pure titanium (cpTi) with a high protein loading (15 wt %) by employing a recently developed wet-chemistry technique. It was observed that the incorporation of BSA significantly modified the morphology, composition, and crystallinity of the Ca-P coating. The Ca-P coating without BSA is a mixture of hydroxyapatite (HA) and octacalcium phosphate (OCP) with sharp-edged thin OCP crystal plates on the top layer, whereas only an HA phase was detected in the Ca-P/BSA coating. The crystal plates in the latter had a more rounded appearance. The Ca-P/BSA coatings were immersed respectively in neutral (pH 7.4) and acidic (starting pH 4.0) phosphate-buffered saline (PBS) at 37°C over a 14-day period. No protein release was detected in the neutral PBS during the immersion; however, a continuous release of BSA was measured in the acidic PBS, subsequently leading to the formation of a very dense and well-adherent composite coating of BSA and Ca-P on cpTi. The present study provides the possibility to achieve a long-term effective release of biologically active proteins from a Ca-P-coated metallic implant. © 1999 John Wiley & Sons, Inc. J Biomed Mater Res, 46, 245–252, 1999.
133 citations
TL;DR: The use of in silico methodologies, peptide databases and software to assess the release of potentially bioactive DPP-IV, renin and ACE-I inhibitory peptides from bovine and porcine meat proteins demonstrating that meat proteins are a suitable resource for the generation of bioactive peptides is demonstrated.
133 citations
TL;DR: All four of the disulfide bonds of α-lactalbumin are shown to be readily available for reduction by 10-3 m dithiothreitol in aqueous buffers at room temperature, and three of the four disulfides are no longer susceptible to reduction.
133 citations
TL;DR: When fat-body tissue from locusts was incubated with palmitate-1-C14 in phosphate-saline, the acid was readily taken up by the tissue; 80-90% of that taken up was esterified and recovered in the glyceride fraction.
133 citations