Dolichyl phosphate-mannosyltransferase and dolichyl phosphate-N-acetylglucosaminyltransferase activities in liver preparations from normal controls and patients with cystic fibrosis and diabetes mellitus.
Publication/Presentation Date
10-31-1983
Abstract
Optimal assay conditions have been determined in human liver preparations for the catalytic transfer of mannose and N-acetylglucosamine from GDP-mannose and UDP-N-acetylglucosamine, respectively, to dolichyl phosphate. Both enzymatic reactions have an absolute requirement for divalent cation (5 mmol/l Mn2+ optimal), detergent (Triton X-100 or Nonidet P-40) and dolichyl phosphate (as acceptor substrate) and both reactions have optimal activity at a pH value of 7.8. Preliminary characterization of the glycolipid products for both enzymatic reactions indicates that phosphorylated dolichol is the major acceptor substrate for radiolabeled mannose and N-acetylglucosamine. The activity levels and specific activities of dolichyl phosphate-mannosyltransferase are comparable in liver homogenates from normal controls and patients with cystic fibrosis and diabetes mellitus. The activity levels and specific activities of dolichyl phosphate-N-acetylglucosaminyltransferase are comparable in liver homogenates from normal controls and patients with cystic fibrosis and diabetes mellitus but considerably lower than the activity levels of dolichyl phosphate-mannosyltransferase. It appears that two of the initial steps of the lipid-mediated glycosylation pathway are normal in livers from patients with cystic fibrosis and diabetes mellitus.
Volume
134
Issue
1-2
First Page
1
Last Page
9
ISSN
0009-8981
Published In/Presented At
Alhadeff, J. A., & Watkins, P. (1983). Dolichyl phosphate-mannosyltransferase and dolichyl phosphate-N-acetylglucosaminyltransferase activities in liver preparations from normal controls and patients with cystic fibrosis and diabetes mellitus. Clinica chimica acta; international journal of clinical chemistry, 134(1-2), 1–9. https://doi.org/10.1016/0009-8981(83)90178-x
Disciplines
Medicine and Health Sciences
PubMedID
6228343
Department(s)
Department of Medicine
Document Type
Article