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J Bacteriol. 1973 February; 113(2): 586-591
Copyright © 1973 American Society for Microbiology. All Rights Reserved.

Acyl Carrier Protein in Mycoplasmas

Department of Clinical Microbiology, The Hebrew University-Hadassah Medical School, Jerusalem, Israel

ABSTRACT

Acyl carrier protein (ACP) activity was determined by the malonyl-coenzyme A–CO₂ exchange reaction. It was highest in Acholeplasma laidlawii, lower in A. granularum, and lowest in A. axanthum. The sterol-requiring Mycoplasma species examined showed little or negligible ACP activity. A. laidlawii was capable of utilizing pantetheine or coenzyme A but not ß-alanine as precursor for ACP synthesis. Its ACP could thus be labeled by growing the organisms with radioactive coenzyme A. The ACP of A. laidlawii appears to be a soluble cytoplasmic protein, which could be purified about 40-fold by treatment of the cytoplasmic fluid with streptomycin sulfate and chromatography of the supernatant fluid on a Biogel P-10 column. Its molecular weight, determined by polyacrylamide gel electrophoresis, is low (about 10,900) resembling that of Escherichia coli, but it is much more sensitive to heat.