Open AccessLow molecular mass products of depolymerization of purified mucin--attempts at isolation and characterization.
Author(s) -
Iwona Minkiewicz,
A Gindzieński
Publication year - 1999
Publication title -
acta biochimica polonica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.452
H-Index - 78
eISSN - 1734-154X
pISSN - 0001-527X
DOI - 10.18388/abp.1999_4115
Subject(s) - mucin , depolymerization , chemistry , proteolysis , acetamide , molecular mass , biochemistry , sodium azide , chromatography , electrophoresis , gel electrophoresis , enzyme , organic chemistry
Samples of crude mucin were incubated at room temperature for 48 and 96 h in a sodium azide containing buffer, pH 7.0. Then each sample was purified, reduced and alkylated with iodo[14C]acetamide. Electrophoretic analysis demonstrated that radioactivity was incorporated into the mucin subunits and proteins of 100 and 140 kDa. The results of our experiments suggest that the released proteins can be a part of mucin molecule, cleaved by proteolysis and reduction of disulfide bridges.