Notizen: Mode of action of O-seryl-N-acetylgalactosaminide glycohydrolase
Open Access
- 1 December 1967
- journal article
- research article
- Published by Walter de Gruyter GmbH in Zeitschrift für Naturforschung B
- Vol. 22 (12), 1357-1358
- https://doi.org/10.1515/znb-1967-1228
Abstract
Experiments indicate that the known resistance of natural ovine submaxillary gland glycoprotein to the enzyme results from steric hindrance by the voluminous N-acetylneuraminic acid unit rather than from the negative charge at its carboxyl group. A [beta]-elimination type of reaction as the mechanism of the action of seryl-N-acetylgalactosaminidase can be excluded.This publication has 5 references indexed in Scilit:
- Studies on glycoproteins XVI. Serine and threonine residues, the only identifiable sugar acceptors in ovine submaxillary gland glycoproteinBiochimica et Biophysica Acta (BBA) - General Subjects, 1967
- Studies on glycoproteins XV. substrate-dependence of O-seryl-O-acetylgalactosaminide glycosidase (Helix pomatia) activity and mechanism of the enzymatic reactionBiochimica et Biophysica Acta (BBA) - General Subjects, 1967
- Studies on glycoproteinsXIII. Preparation of ovine submaxillary gland glycoprotein by gel filtration and its physical, chemical and immunochemical characterizationBiochimica et Biophysica Acta (BBA) - General Subjects, 1966
- Studies on glycoproteins XI. The O-glycosidic linkage of N-acetylgalactosamine to seryl and threonyl residues in ovine submaxillary gland glycoproteinBiochimica et Biophysica Acta (BBA) - Mucoproteins and Mucopolysaccharides, 1965
- A MODIFIED COLORIMETRIC METHOD FOR THE ESTIMATION OF N-ACETYLAMINO SUGARSJournal of Biological Chemistry, 1955