Matches in SemOpenAlex for { <https://semopenalex.org/work/W2005189637> ?p ?o ?g. }
Showing items 1 to 70 of
70
with 100 items per page.
- W2005189637 endingPage "70" @default.
- W2005189637 startingPage "66" @default.
- W2005189637 abstract "Rabbit skeletal muscle glycogen synthetase exists in two forms, the non-phosphorylated, glucose 6-phosphate-independent I-form and the phosphorylated, glucose 6-phosphate-dependent D-form. The conversion of the I-form to the D-form can be effected by phosphorylation catalyzed by either cyclic AMP-dependent [ 1,2] or cyclic AMP-independent [3-51 protein kinases and by limited proteolytic digestion [6-91, whereas conversion brought about by phosphorylation can be reversed by the action of phosphoprotein phosphatase(s), that due to proteases is irreversible. Takeda and Larner [8] and Soderling [9] reported that the conversion of synthetase I to synthetase D by trypsin is accompanied by a decrease in the molecular weight from 90 000 to about 75 000. Takeda and Lamer [8] further reported that the action of trypsin on synthetase is restricted to the COOH-terminal part of the molecule. This report is concerned with further examination of the effect of proteolysis digestion on glycogen synthetase structure and activity using subtilisin as well as trypsin for this purpose. A striking feature of the effect of subtilisin is a marked activation of the enzyme that occurs during the early part of the reaction as seen by activity determinations carried out in the presence or absence of glucose 6-phosphate. In the course of this work the amino acid sequence of the NH2 -terminal portion of the synthetase was determined and found to be slightly different from that reported [lo]. It was noted that low levels of either trypsin or subtilisin cause some modification of the NH2 -terminal region of the synthetase." @default.
- W2005189637 created "2016-06-24" @default.
- W2005189637 creator A5007665730 @default.
- W2005189637 creator A5078244774 @default.
- W2005189637 date "1979-02-01" @default.
- W2005189637 modified "2023-09-27" @default.
- W2005189637 title "Effect of proteases on the structure and activity of rabbit skeletal muscle glycogen synthetase" @default.
- W2005189637 cites W1517593659 @default.
- W2005189637 cites W1979684936 @default.
- W2005189637 cites W1991081285 @default.
- W2005189637 cites W2001866120 @default.
- W2005189637 cites W2013851566 @default.
- W2005189637 cites W2051794029 @default.
- W2005189637 cites W2058613232 @default.
- W2005189637 cites W2093551858 @default.
- W2005189637 doi "https://doi.org/10.1016/0014-5793(79)80153-2" @default.
- W2005189637 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/107043" @default.
- W2005189637 hasPublicationYear "1979" @default.
- W2005189637 type Work @default.
- W2005189637 sameAs 2005189637 @default.
- W2005189637 citedByCount "27" @default.
- W2005189637 crossrefType "journal-article" @default.
- W2005189637 hasAuthorship W2005189637A5007665730 @default.
- W2005189637 hasAuthorship W2005189637A5078244774 @default.
- W2005189637 hasConcept C105795698 @default.
- W2005189637 hasConcept C134018914 @default.
- W2005189637 hasConcept C181199279 @default.
- W2005189637 hasConcept C182220744 @default.
- W2005189637 hasConcept C185592680 @default.
- W2005189637 hasConcept C192118531 @default.
- W2005189637 hasConcept C2777499176 @default.
- W2005189637 hasConcept C2779884254 @default.
- W2005189637 hasConcept C2779959927 @default.
- W2005189637 hasConcept C33923547 @default.
- W2005189637 hasConcept C55493867 @default.
- W2005189637 hasConcept C86803240 @default.
- W2005189637 hasConceptScore W2005189637C105795698 @default.
- W2005189637 hasConceptScore W2005189637C134018914 @default.
- W2005189637 hasConceptScore W2005189637C181199279 @default.
- W2005189637 hasConceptScore W2005189637C182220744 @default.
- W2005189637 hasConceptScore W2005189637C185592680 @default.
- W2005189637 hasConceptScore W2005189637C192118531 @default.
- W2005189637 hasConceptScore W2005189637C2777499176 @default.
- W2005189637 hasConceptScore W2005189637C2779884254 @default.
- W2005189637 hasConceptScore W2005189637C2779959927 @default.
- W2005189637 hasConceptScore W2005189637C33923547 @default.
- W2005189637 hasConceptScore W2005189637C55493867 @default.
- W2005189637 hasConceptScore W2005189637C86803240 @default.
- W2005189637 hasIssue "1" @default.
- W2005189637 hasLocation W20051896371 @default.
- W2005189637 hasLocation W20051896372 @default.
- W2005189637 hasOpenAccess W2005189637 @default.
- W2005189637 hasPrimaryLocation W20051896371 @default.
- W2005189637 hasRelatedWork W1873278284 @default.
- W2005189637 hasRelatedWork W1883802169 @default.
- W2005189637 hasRelatedWork W1982909042 @default.
- W2005189637 hasRelatedWork W2033092971 @default.
- W2005189637 hasRelatedWork W2052565523 @default.
- W2005189637 hasRelatedWork W2099748948 @default.
- W2005189637 hasRelatedWork W2103738707 @default.
- W2005189637 hasRelatedWork W2181666426 @default.
- W2005189637 hasRelatedWork W2311319429 @default.
- W2005189637 hasRelatedWork W2882971477 @default.
- W2005189637 hasVolume "98" @default.
- W2005189637 isParatext "false" @default.
- W2005189637 isRetracted "false" @default.
- W2005189637 magId "2005189637" @default.
- W2005189637 workType "article" @default.