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- W2000286608 abstract "The major bovine seminal plasma protein, PDC-109 exhibits chaperone-like activity (CLA) against a variety of target proteins. The present studies show that the homologous protein from equine seminal plasma, HSP-1/2 also exhibits CLA and inhibits the thermal aggregation of target proteins such as lactate dehydrogenase, and DTT-induced aggregation of insulin in a concentration-dependent manner. Phosphorylcholine binding inhibited the CLA of HSP-1/2, suggesting that aggregation state of the protein is important for this activity. These results demonstrate that HSP-1/2 functions as a molecular chaperone in vitro, and suggest that it may protect other proteins of equine seminal plasma from unfolding/misfolding or aggregation. These results suggest that homologous proteins from the seminal plasma of other mammals also exhibit CLA, which will be physiologically relevant." @default.
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- W2000286608 date "2012-10-01" @default.
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- W2000286608 title "HSP-1/2, a major protein of equine seminal plasma, exhibits chaperone-like activity" @default.
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- W2000286608 doi "https://doi.org/10.1016/j.bbrc.2012.08.120" @default.
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