| Two glycogen synthase activities associated with proteoglycogen in retina. | |
| | |
MedLine Citation:
|
PMID: 10685612 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
|
Glycogen synthase of bovine retina was found associated with the acid-insoluble and acid-soluble proteoglycogen fractions. The synthase associated with the acid-insoluble proteoglycogen precursor showed an 8-fold lower Km for UDP-glucose than the synthase associated with the acid-soluble fraction, and was inhibited by detergent. A short digestion with pronase resulted in conversion of the acid insoluble fraction into acid-soluble. The results lead us to postulate that the acid-insolubility of the proteoglycogen fraction and the association with retina membrane proposed before, is caused by glycogen synthase strongly associated to its polysaccharide moiety. The enlargement of the polysaccharide moiety during proteoglycogen biosynthesis, from glycogenin linked to a few 11 to 12 glucose units to the acid-insoluble proteoglycogen precursor (Mr 470,000) would be carried out, together with the branching enzyme, by the glycogen synthase showing a low Km for UDP-glucose. The glycogen synthase with the highest Km for UDP-glucose would participate in conversion of the precursor into mature acid-soluble proteoglycogen. |
| | |
Authors:
|
J A Curtino; E R Lacoste |
Publication Detail:
|
Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
|
Title: Neurochemical research Volume: 25 ISSN: 0364-3190 ISO Abbreviation: Neurochem. Res. Publication Date: 2000 Jan |
Date Detail:
|
Created Date: 2000-03-09 Completed Date: 2000-03-09 Revised Date: 2006-11-15 |
Medline Journal Info:
|
Nlm Unique ID: 7613461 Medline TA: Neurochem Res Country: UNITED STATES |
Other Details:
|
Languages: eng Pagination: 129-32 Citation Subset: IM |
Affiliation:
|
Centro de Investigaciones en Química Biológica de Córdoba (CIQUIBIC), UNC-CONICET, Departamento de Química Biológica Dr. Ranwel Caputto, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Argentina. jcurtino@dqbfcq.uncor.edu |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
Animals Cattle Detergents / pharmacology Enzyme Inhibitors / pharmacology Glucosyltransferases Glycogen Synthase / antagonists & inhibitors, metabolism* Glycoproteins / chemistry, metabolism* Glycosylation Hydrogen-Ion Concentration Polysaccharides / chemistry, metabolism* Pronase / metabolism Retina / enzymology* Solubility Trichloroacetic Acid Uridine Diphosphate Glucose / metabolism |
| Chemical | |
Reg. No./Substance:
|
0/Detergents; 0/Enzyme Inhibitors; 0/Glycoproteins; 0/Polysaccharides; 0/glycogenin; 133-89-1/Uridine Diphosphate Glucose; 76-03-9/Trichloroacetic Acid; EC 2.4.1.-/Glucosyltransferases; EC 2.4.1.11/Glycogen Synthase; EC 3.4.24.-/Pronase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Kinetics of Na+, K+-ATPase inhibition by an endogenous modulator (II-A).
Next Document: Scinderin, a Ca2+-dependent actin filament severing protein that controls cortical actin network dyn...