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. 1971 Apr;21(4):639-42.
doi: 10.1128/am.21.4.639-642.1971.

Tetracycline inhibition of a lipase from Corynebacterium acnes

K Weaber, R Freedman, W W Eudy

Tetracycline inhibition of a lipase from Corynebacterium acnes

K Weaber et al. Appl Microbiol. 1971 Apr.

Abstract

A lipase which hydrolyzes triglycerides (tricaprylin and trilaurin) and naphthyl laurate was obtained from the broth of Corynebacterium acnes cultures by ammonium sulfate fractionation. Ca(2+) and sodium taurocholate stimulated activity of the enzyme. Ethylenediaminetetraacetic acid (EDTA) did not inhibit activity of the Ca(2+)-activated enzyme, but lipolytic activity was inhibited by EDTA in the absence of Ca(2+). Tetracycline (10(-4)m) produced a slight inhibition of the lipase activity with 5 x 10(-5)m or less showing no effect on the lipase activity. However, complete inhibition by tetracycline at 10(-4)m was observed for Ca(2+)-activated enzyme. Tetracycline inhibition of the C. acnes lipase could be demonstrated at concentrations as low as 10(-6)m.

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