The presence of glycosyltransferases on chromatin acceptors in monkey liver nuclear membranes (author's transl)

Nuclei were prepared from monkey hepatocytes by centrifugation of the homogenate on a cushion of 2.3 M sucrose, during 45 min at 100000 X g. The yield was 2.2 x 10(7) nuclei per g of liver, and 70% of te homogenate DNA was recovered in these nuclei. An electron microscopic study as well as a biochemical analysis of marker enzymes showed that the nuclei are not contaminated by other subcellular fractions, especially endoplasmic reticulum. A mannosyltransferase and an N-acetylglucosaminyltransferase, working on endogenous glycoproteic acceptors, are present in the nuclei for 1.4 and 6.5% of the homogenate activities, respectively. The nuclei are hydrolysed by DNAse I. The suspension, adjusted in 1.9 M sucrose, was centrifuged for 2 h at 100000 X g, under buffer layer. Purified nuclear membranes were collected at the interface. These membranes did not contain any more endoplasmic reticulum enzyme activities, but the mannosyl and N-acetylglucosaminyltransferase activities were still present. They essentially work on an exogenous chromatin acceptor, prepared by lysis of the nuclei. The eventual role of these glycosyltransferases in the glycosylation of non-histone proteins is discussed.

Medienart:

Artikel

Erscheinungsjahr:

1980

Erschienen:

1980

Enthalten in:

Zur Gesamtaufnahme - volume:603

Enthalten in:

Biochimica et biophysica acta - 603(1980), 2 vom: 12. Dez., Seite 245-54

Sprache:

Französisch

Weiterer Titel:

Présence de glycosyltransferases à accepteurs chromatiniens dans les membranes nucléaires d'hépatocytes de singe

Beteiligte Personen:

Berthillier, G [VerfasserIn]
Benedetto, J P [VerfasserIn]
Got, R [VerfasserIn]

Themen:

Acetylglucosamine
Chromatin
EC 2.4.1.-
EC 2.4.1.150
English Abstract
Glucosyltransferases
Hexosyltransferases
Journal Article
Mannosyltransferases
N-Acetylglucosaminyltransferases
N-acetyllactosaminide beta-1,6-N-acetylglucosaminyltransferase
V956696549

Anmerkungen:

Date Completed 24.04.1981

Date Revised 09.06.2019

published: Print

Citation Status MEDLINE

Förderinstitution / Projekttitel:

PPN (Katalog-ID):

NLM064276090