Renal γ-glutamyl transpeptidases: Influence of glycosylation on the electrophoretic behavior and molecular weights of their subunits Academic Article Article uri icon

Overview

MeSH Major

  • Carrier Proteins
  • Cell Membrane
  • Endoplasmic Reticulum
  • Mitochondrial Proteins
  • Saccharomyces cerevisiae Proteins
  • Sterols

abstract

  • The molecular weights (Mr) of mammalian renal gamma-glutamyl transpeptidase light subunits vary from 21 to 25 K; a much broader range is seen for the large subunit (51 to 72 K). However, chemical deglycosylation of these enzymes (rat, human, and bovine) yields subunits each of which exhibits identical Mr (41 and 19 K for the heavy and light subunits, respectively), suggesting strong similarity between the peptide backbones of these glycoproteins. Immunological data also indicate homologies between these enzymes. The difference observed in the Mr of native subunits thus seem to be related to the extent and nature of glycosylation of these proteins.

publication date

  • December 30, 1986

Research

keywords

  • Academic Article

Identity

Digital Object Identifier (DOI)

  • 10.1016/S0006-291X(86)80170-X

PubMed ID

  • 2434082

Additional Document Info

start page

  • 1189

end page

  • 94

volume

  • 141

number

  • 3