Unknown

Dataset Information

0

A 70000-molecular-weight protein isolated from purified pig gastric mucus glycoprotein by reduction of disulphide bridges and its implication in the polymeric structure.


ABSTRACT: The glycoprotein of pig gastric mucus has been isolated free of non-covalently bound protein as judged by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and equilibrium density-gradient centrifugation. After reduction with 0.2 M-mercaptoethanol, protein was released from the glycoprotein, which consisted of a major 70000-mol.wt. component and a minor 60000-mol.wt. component. The 70000-mol.wt. protein fraction was separated from the reduced glycoprotein by either density-gradient centrifugation in CsCl or by gel filtration. Analysis of the 70000-mol.wt. protein fraction showed that, within the limits of the analysis, it was non-glycosylated, and its amino acid analysis was quite different from that of the reduced glycoprotein, which is high in serine, threonine and proline. There was a ratio of one 70000-mol.wt. protein per native glycoprotein molecule of 2 X 10(6) mol.wt. Dissociation of the native glycoprotein into glycoprotein subunits (5 X 10(5) mol.wt.) by reduction or proteolysis results in the release or hydrolysis respectively of the 70000-mol.wt. protein. A similar 70000-mol.wt. protein is demonstrated in human gastric mucus glycoprotein. A structural role for the proteins in these mucus glycoproteins is proposed.

SUBMITTER: Pearson JP 

PROVIDER: S-EPMC1163065 | biostudies-other | 1981 Jul

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC1162883 | biostudies-other
| S-EPMC1152455 | biostudies-other
| S-EPMC1152144 | biostudies-other
| S-EPMC1144973 | biostudies-other
| S-EPMC4488071 | biostudies-literature
| S-EPMC1270086 | biostudies-other
| S-EPMC1164705 | biostudies-other
| S-EPMC1148212 | biostudies-other
| S-EPMC3380823 | biostudies-literature
| S-EPMC1185811 | biostudies-other