Premium
Gel electrophoresis salivary mucins
Author(s) -
Kashket Shelby,
Ciociolo James M.
Publication year - 1981
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150020109
Subject(s) - mucin , sialic acid , agarose , glycoprotein , chemistry , gel electrophoresis , polyacrylamide gel electrophoresis , electrophoresis , biochemistry , chromatography , mucus , agarose gel electrophoresis , gel electrophoresis of proteins , microbiology and biotechnology , biology , enzyme , ecology , gene
Bovine Submaxillary mucin (BSM) and human submandibular mucin (HSM) were electrophoresed in a system in which the mucins were incorporated into an agarose sample gel and separation was carried out in a 5 % polyacrylamide gel. BSM was resolved into two protein‐ and carbohydrate‐containing bands, and a number of non‐mucin proteins. When the electrophoresis was carried out at 80°C, the mobilities and resolution of the bands were increased. The entry of HSM into the running gel was also increased at the elevated temperature and the samples were separated into at least four protein‐ and carbohydrate‐stainable bands. Protein bound sialic acid remained unchanged unter these conditions and aggregating activity for cells of a strain of oral streptococcus could be recovered from the gels after the electrophoresis. The facilitation of the electrophoresis of human mucus glycoprotein's at high temperature may reflect the dissociation of macromolecular aggregates of the mucins under these conditions. A number of purified, non‐mucin proteins also moved as discrete bands at 80degreeC. It is suggested that electrophoresis at elevated temperatures should be considered generally for the analysis of multimolecular systems that are of biological importance.