Rat liver microsomal palmitoyl-CoA synthetase: Subunit structure

Eddie Maes*, Jacob Bar-Tana

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

Abstract

Long chain fatty acyl-CoA synthetase (acid:CoA ligase (AMP-forming), EC 6.2.1.3) from rat liver microsomes was shown to dissociate completely into one polypeptide chain in 75% 2-chloroethanol in water. The presence of one amino and one carboxy terminal was established. The molecular weight of the subunit as deduced from sedimentation equilibrium as well as quantitative carboxy terminal analysis agrees with the value of 28 000 ± 1000 as reported previously (Bar-Tana, J. and Rose, G. (1973) Biochem. J. 131, 443-449). Hence, the catalytic unit of 168 000 daltons appears to be composed of identical subunits.

Original languageEnglish
Pages (from-to)527-530
Number of pages4
JournalBBA - Enzymology
Volume480
Issue number2
DOIs
StatePublished - 9 Feb 1977

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