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PROPERTIES OF PURIFIED PHOSPHOLIPASE C FROM ACINETOBACTER CALCOACETICUS
Author(s) -
Lehmann Vidar
Publication year - 1973
Publication title -
acta pathologica microbiologica scandinavica section b microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.909
H-Index - 88
eISSN - 1600-0463
pISSN - 0365-5563
DOI - 10.1111/j.0365-5563.1973.tb00008.x
Subject(s) - chromatography , phosphatidylethanolamine , lecithin , acinetobacter calcoaceticus , chemistry , sphingomyelin , phosphatidylcholine , isoelectric point , sephadex , enzyme , phospholipase , phosphatidylserine , hydrolysis , biochemistry , ultrafiltration (renal) , albumin , phospholipid , acinetobacter , cholesterol , membrane , antibiotics
Phospholipase C (phosphatidylcholine cholinephosphohydrolase, EC 3.1.4.3) from Acinetobacter calcoaceticus was purified 20‐fold by ultrafiltration and chromatography on DEAE‐Sephadex. The purified enzyme was markedly labile. Mg 2+ , deoxycholate and albumin enhanced the enzymatic activity against lecithin, while Ca 2+ , Zn 2+ and ethylendiaminetetraacetate inhibited the activity. The temperature coefficient (Q 10°C ) was 1.7 and optimum pH 8.2–8.6. The Michaelis constant was found to be lower than 250 μ M. At pH 8.3, lecithin, phosphatidylethanolamine, phosphatidylserine and sphingomyelin were attacked, while at pH 6.3 only lecithin and sphingomyelin were susceptible to hydrolysis.