Hydrolysis of synthetic phosphatides by clostridium welchii phosphatidase

Deenen, L.L.M. Van; Haas, G.H. de; Heemskerk, C.H.Th.; Meduski, J

doi:10.1016/0006-291x(61)90267-4

Cited by 21 publications

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“…After the discovery by Macfarlane & Knight (1941) that the haemolytic factor of Clostridium welchii a-toxin converted lecithins into phosphorylcholine and diglycerides, it was established that sphingomyelins are hydrolysed at a considerably lower rate, whereas isolated kephalins and synthetic phosphatidylethanolamines appeared not to be susceptible at all (Zamecnik, Brewster & Lipmann, 1947; Macfarlane, 1948;van Deenen, de Haas, Heemskerk & Meduski, 1961). The action of this enzyme has been investigated in red cells of different species of mammals (man, rat, rabbit, pig, 34P PROCEEDINGS OF THE BIOCHEMICAL SOCIETY ox), which are known to differ greatly with respect to their phosphatide composition.…”

Section: Pmentioning

confidence: 99%

Proceedings of The Biochemical Society

1961

Biochemical Journal

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Two water-soluble phospholipases have been investigated: (1) the lecithin-splitting activity of Penicillium notatum phospholipase B, and (2) the phospholipase C (cx-toxin) of Clostridium perfringens. The rate of enzymic hydrolysis has been related to the electrokinetic properties of the phospholipid substrate particles. The c-potential of such particles (e.g. lecithin micelles) has been varied by adding amphipathic molecules to the micelles (i.e. longchain bases or acids) while the c-potential of both substrate and enzyme has been changed by introducing polyvalent ions, e.g. Ca2+ or Fe(CN)683-, into

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Section: Pmentioning

confidence: 99%