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. 1973 Feb;113(2):586–591. doi: 10.1128/jb.113.2.586-591.1973

Acyl Carrier Protein in Mycoplasmas

Shlomo Rottem 1, Ofra Muhsam-Peled 1, Shmuel Razin 1
PMCID: PMC285269  PMID: 4570599

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 β-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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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