Literature DB >> 827218

Carbohydrate moieties of human seminal plasma arylamidases.

W P Herrmann, G Uhlenbruck.   

Abstract

Human seminal plasma contains two arylamidases that differ considerably with respect to their antigenic structures, molecular weights and electrophoretic mobilities. Both enzymes are glycoproteins with different carcohydrate moieties. With the aid of precipitating lectins, the faster migrating arylamidase I was found to possess a PHA receptor (beta-Gal-GNAc-(Man)2-GNAc) with terminal N-acetyl-neuraminic acid groups. The carbohydrate moiety of arylamidase II consists of at least 2 types of carbohydrate chains: A disaccharide (beta-Gal(1-3)GalNAc) reacting with the lectin from Arachis hypogoea and in addition a chain containing the PHA receptor. This chain probably contains a terminal neuraminic acid group and a terminal fucosly group.

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Year:  1976        PMID: 827218     DOI: 10.1111/j.1439-0272.1976.tb01661.x

Source DB:  PubMed          Journal:  Andrologia        ISSN: 0303-4569            Impact factor:   2.775


  2 in total

1.  Immunological characterization of an arylamidase (aminopeptidase) occurring in histiocytoma.

Authors:  W P Herrmann; I Schneider
Journal:  Arch Dermatol Res       Date:  1976-06-21       Impact factor: 3.017

2.  Incomplete arylamidase in psoriasis scales.

Authors:  W P Herrmann
Journal:  Arch Dermatol Res       Date:  1976-06-21       Impact factor: 3.017

  2 in total

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