1887

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Volume 1, Issue 3

The Lecithinase of and its Relation to the a-toxin of Free

Abstract

SUMMARY : elaborates a lecithinase which induces turbidity and curding in crude lecithovitellin preparations, and hydrolyzes egg-yolk lecithin with the liberation of acid-soluble phosphate, both over a pH range of 50–63 with a maximum in the region of pH 6·0. It does not induce turbidity in human serum alone, but does so in the presence of agar gels, which activate the reaction over a pH range of 50·80. The activities are not dependent on the presence of Ca ions. The enzyme responsible appears to be a lecithinase C.

In the concentration available the lecithinase haemolysed rabbit and mouse, but not human, horse, sheep or guinea-pig red cells; and it was not lethal on intravenous injection into mice, but was slightly toxic in the skin of guinea-pigs.

The lecithinase C is antigenically related to the lecithinase C (the α-toxin) of , though differing from the α-toxin in its pH optima, haemolytic powers, independence of Ca ions and relative non-toxicity. It is neutralized by α-antitoxin, and antilecithinase behaves in a reciprocal manner, neutralizing the lecithinase, necrotizing and lethal action of α-toxin. The antigenic relation of the two lecithinases appears to be remote.

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© Society for General Microbiology, 1947
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1947-09-01
2024-04-18
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The Lecithinase of Clostridium bifermentans and its Relation to the a-toxin of Clostridium welchii
Microbiology 1, 385 (1947); https://doi.org/10.1099/00221287-1-3-385
/content/journal/micro/10.1099/00221287-1-3-385
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