Literature DB >> 2578983

The carbohydrate moiety of aminopeptidase N of rabbit intestinal brush-border membrane.

D Massey, S Maroux.   

Abstract

Endoglycosidase F was used to eliminate the N-linked complex glycans from intestinal aminopeptidase N. The glycans which were probably O-linked remaining after the endoglycosidase F treatment exhibited the human blood group A and H determinants expressed in enzymes from A+ or A- rabbits, respectively. The molecular mass estimation of the two types of glycans by SDS-polyacrylamide gel electrophoresis and the sugar composition of aminopeptidase from A+ and A- rabbits strongly suggested the presence of eight N-linked complex glycans and two O-linked oligosaccharides bearing the human group antigenicity.

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Year:  1985        PMID: 2578983     DOI: 10.1016/0014-5793(85)80261-1

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  2 in total

1.  Evidence for the transit of aminopeptidase N through the basolateral membrane before it reaches the brush border of enterocytes.

Authors:  D Massey; H Feracci; J P Gorvel; A Rigal; J M Soulié; S Maroux
Journal:  J Membr Biol       Date:  1987       Impact factor: 1.843

2.  Biosynthesis of intestinal microvillar proteins. Processing of N-linked carbohydrate is not required for surface expression.

Authors:  E M Danielsen; G M Cowell
Journal:  Biochem J       Date:  1986-12-15       Impact factor: 3.857

  2 in total

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