Binding of sodium dodecyl sulfate to aprotinin and its effect on the aprotinin molecule

Shikimi, T.

Chemical and Pharmaceutical Bulletin 34(5): 2224-2227


ISSN/ISBN: 0009-2363
PMID: 2427229
DOI: 10.1248/cpb.34.2224
Accession: 039389617

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When the basic protease inhibitor aprotinin was treated with sodium dodecyl sulfate (SDS), it showed an increased apparent molecular weight upon SDS gel electrophoresis. The amount of SDS bound to aprotinin was much lower than that bound to aprotinin treated with SDS and mercaptoethanol (ME). This result suggests that the increased apparent molecular weight upon SDS gel electrophoresis is not due to dimerization of aprotinin in the presence of SDS, but rather derives from a decrease of SDS binding to aprotinin. Aprotinin treated with SDS retained both the inhibitory activity against trypsin and immunoreactivity against antiaprotinin immunoglobulin G (IgG), whereas aprotinin treated with SDS and ME showed no inhibitory activity against trypsin but did retain immunoreactivity against antiaprotinin IgG. These observations indicate that aprotinin resists denaturation by SDS, but is considerably affected by treatment with SDS and ME.