Abstract
Native polyacrylamide gel electrophoresis (N-PAGE) is a simple qualitative technology to determine heterogeneity of proteins. Here, we have applied N-PAGE to examine heat-induced aggregation and oligomerization of bovine serum albumin (BSA) and the effects of temperature, caprylic acid, N-acetyl-tryptophan, DNA, arginine and gallic acid. Arginine showed marginal protection of BSA against heat-induced aggregation and oligomerization, while other compounds showed varying degree of protections. It is interesting to point out that new bands were formed in the presence of some of these compounds upon heating. Among the compounds tested, gallic acid showed protection of monomeric BSA (observed in N-PAGE as a prominent band) and increased the mobility of native BSA. The increased mobility indicates binding of gallic acid to the native BSA.
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