Phospholipase C from Bacillus cereus. Action on Some Artificial Lecithins.
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چکیده
منابع مشابه
Purification by affinity chromatography of phospholipase C from Bacillus cereus.
Phospholipase C (phosphatidylcholine cholinephosphohydrolase, EC 3.1.4.3) is a bacterial enzyme widely used in membrane and phospholipid studies. For such studies the highest possible degree of purity is required. Both the Bacillus cereus and the Clostridium perfringens enzymes have been purified to apparent homogeneity using conventional techniques [l-3]. However, using a phospholipase C-hyper...
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Phospholipase C activity present in the growth medium of Bacillus ceyeus was purified 2o-fold by chromatography on polyethyleneimine-cellulose columns, or by treatment with protamine sulfate and subsequent chromatography on DEAE-cellulose columns. Purified enzyme preparations retained the ability to hydrolyze ethanolamine phosphoglycerides in the absence of choline phosphoglycerides. A typical ...
متن کاملThe histidine residues of phospholipase C from Bacillus cereus.
The inactivation of phospholipase C from Bacillus cereus at pH6 by diethyl pyrocarbonate parallelled the N-ethoxyformylation of a single histidine residue in the enzyme. The inactivation arose from a decrease in the maximum velocity of the enzymic reaction with no effect on the Km value. The inactivation did not apparently alter the ability of the enzyme to bind to a substrate-based affinity ge...
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The rate of phospholipid hydrolysis in erythrocyte ghosts by Bacillus cereus phospholipase C was markedly decreased by the presence of NaCl at concentrations between 25 and 200 mM. The inhibition seemed to be due to Cl- and was unaffected by the type of cation present. The larger univalent anions such as HCO3-, Br-, Cl-, NO3-, CNO- and I- seemed most effective, whereas the bivalent anion SO42- ...
متن کاملPurification of phospholipase C from Bacillus cereus by hydrophobic chromatography on palmitoyl cellulose.
Phospholipase C (phosphatidylcholine choline-phosphohydrolase, EC 3.1.4.E) from Bacillus cereus (IAM-1208) was adsorbed to palmitoyl cellulose from a crude enzyme solution at pH 5--9. The adsorption was not influenced by ionic strength up to 2 M NaCl. The adsorbed enzyme was eluted almost completely by washing the cellulose with a suitable detergent, such as Triton X-100, Adekatol SO-120, Catio...
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ژورنال
عنوان ژورنال: Acta Chemica Scandinavica
سال: 1977
ISSN: 0904-213X
DOI: 10.3891/acta.chem.scand.31b-0267