Literature DB >> 3094592

[The presence of glycogen synthase in phosphorylase kinase preparations isolated from rabbit skeletal muscles].

S A Shur, L K Skolysheva, P L Vul'fson.   

Abstract

Phosphorylase kinase isolated from rabbit skeletal muscle contains a protein whose molecular mass as determined by polyacrylamide gel electrophoresis is 571 000 Da. The protein was found to possess a higher affinity for glycogen as compared to phosphorylase kinase and phosphorylase. The protein separated from kinase by chromatography on a DEAE-cellulose column produced during SDS electrophoresis one protein band corresponding to Mr of 95 200 Da. The above properties of the protein and the glycogen synthetase activity revealed in the presence of glucose-6-phosphate suggest that phosphorylase kinase preparations contain a hexameric form of glycogen synthetase.

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Year:  1986        PMID: 3094592

Source DB:  PubMed          Journal:  Biokhimiia        ISSN: 0320-9725


  1 in total

1.  An abundant and ubiquitous homo-oligomeric ring-shaped ATPase particle related to the putative vesicle fusion proteins Sec18p and NSF.

Authors:  J M Peters; M J Walsh; W W Franke
Journal:  EMBO J       Date:  1990-06       Impact factor: 11.598

  1 in total

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