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Poly( N ‐Acetyllactosaminyl) Oligosaccharides of Chromaffin Granule Membrane Glycoproteins
Author(s) -
Margolis Richard U.,
FischerColbrie Reiner,
Margolis Renée K.
Publication year - 1988
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1988.tb01163.x
Subject(s) - glycoprotein , granule (geology) , biochemistry , gel electrophoresis , chemistry , polyacrylamide gel electrophoresis , molecular mass , membrane glycoproteins , enzyme , biology , paleontology
Poly( N ‐acetyllactosaminyl) oligosaccharides have been identified, on the basis of their susceptibility to endo‐β‐galactosidase, in a large‐molecular‐size glycopeptide fraction derived from chromaffin granule membrane glycoproteins. The glycoproteins containing poly( N ‐acetyl‐lactosaminyl) oligosaccharides were selectively labeled by treatment of chromaffin granule membranes with endo‐β‐galactosidase to expose N ‐acetylglucosamine residues, followed by incubation with galactosyltransferase and UDP‐[ 14 C]galactose. Sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE) and fluorography demonstrated specific labeling in the 41–47 kilodalton (kD) region and in a distinct band at 90 kDa. Two‐dimensional SDS‐PAGE revealed that the poly( N ‐acetyllactosaminyl) oligosaccharides are predominantly present in glycoprotein IV, together with lesser labeling of glycoproteins II and III, whereas they are absent from dopamine β‐hydroxylase and carboxypeptidase H, which are the major glycoproteins of chromaffin granule membranes.