Low molecular mass products of depolymerization of purified mucin--attempts at isolation and characterization.
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.
Minkiewicz
I
I
Department of General and Organic Chemistry, Institute of Chemistry, Medical Academy of Białystok, Poland.
Gindzieński
A
A
D000478:Alkylation; D000818:Animals; D001345:Autoradiography; D002850:Chromatography, Gel; D004220:Disulfides / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D005752:Gastric Mucins / Q000737:chemistry* / Q000302:isolation & purification*; D008970:Molecular Weight; D010084:Oxidation-Reduction; D020836:Protein Structure, Quaternary; D013552:Swine
D004220:Disulfides; D005752:Gastric Mucins