Acyl-coenzyme A carboxylase of the free-living nematode Turbatrix aceti. 1. Its isolation and molecular characteristics
- 1 May 1978
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 17 (10), 1822-1827
- https://doi.org/10.1021/bi00603a003
Abstract
A biotin containing enzyme which carboxylates acetyl-CoA was isolated from the nematode T. aceti and purified to homogeneity as judged by the criteria of polyacrylamide gel electrophoresis and ultracentrifugation. The enzyme has a sedimentation coefficient of 18.0 S and a MW of 667,000. It is composed of 4 protomers having a MW of 140,000 each. Each protomer in turn consists of 2 distinct polypeptide chains (MW 82,000 and 58,000) and 1 biotinyl prosthetic group linked to the 82,000 peptide. The amino acid composition of the nematode carboxylase was determined.This publication has 8 references indexed in Scilit:
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