Literature DB >> 2559137

Functional size of acyl coenzyme A:diacylglycerol acyltransferase by radiation inactivation.

S Ozasa1, E S Kempner, S K Erickson.   

Abstract

Rat liver acyl coenzyme A:diacylglycerol acyltransferase, an intrinsic membrane activity associated with the endoplasmic reticulum, catalyzes the terminal and rate-limiting step in triglyceride synthesis. This enzyme has never been purified nor has its gene been isolated. Inactivation by ionizing radiation and target analysis were used to determine its functional size in situ. Monoexponential radiation inactivation curves were obtained which indicated that a single-sized unit of 72 +/- 4 kDa is required for expression of activity. The size corresponds only to the protein portion of the target and may represent one or several polypeptides.

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Year:  1989        PMID: 2559137

Source DB:  PubMed          Journal:  J Lipid Res        ISSN: 0022-2275            Impact factor:   5.922


  3 in total

1.  A protein tyrosine kinase associated with the ATP-dependent inactivation of adipose diacylglycerol acyltransferase.

Authors:  T E Lau; M A Rodriguez
Journal:  Lipids       Date:  1996-03       Impact factor: 1.880

2.  Purification, molecular cloning, and expression of the mammalian sigma1-binding site.

Authors:  M Hanner; F F Moebius; A Flandorfer; H G Knaus; J Striessnig; E Kempner; H Glossmann
Journal:  Proc Natl Acad Sci U S A       Date:  1996-07-23       Impact factor: 11.205

3.  Identification of a gene encoding an acyl CoA:diacylglycerol acyltransferase, a key enzyme in triacylglycerol synthesis.

Authors:  S Cases; S J Smith; Y W Zheng; H M Myers; S R Lear; E Sande; S Novak; C Collins; C B Welch; A J Lusis; S K Erickson; R V Farese
Journal:  Proc Natl Acad Sci U S A       Date:  1998-10-27       Impact factor: 11.205

  3 in total

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