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- W2054184685 abstract "1.1. Freshly prepared homogenates of pig pancreatic tissue contain a small amount of phospholipase A (phosphatide acyl-hydrolase, EC 3.1.1.4); during autolysis, however, a considerable rise in lipolytic activity occurs.2.2. By use of heat treatment, (NH4)2SO4 precipitation and chromatographic procedures, the enzyme has been purified about 200 times and characterized by chemical and enzymatic procedures.3.3. The protein, which has a molecular weight of about 13 800 ± 500 appears to consist of one single polypeptide chain terminating in alanine (NH2) and cystine (COOH), and cross-linked intramolecularly by 7 disulphide bridges.4.4. The enzyme acts stereospecifically on all common types of 3-sn-phosphoglycerides, hydrolysing exclusively fatty acid ester bonds at the glycerol-C-2 position, regardless of chain length or degree of unsaturation. In contrast to the snake venom phospholipase A, the pancreatic enzyme shows a marked preference for anionic phospholipids such as phosphatidic acid, cardiolipin and phosphatidyl glycerol." @default.
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- W2054184685 date "1968-04-01" @default.
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- W2054184685 title "Purification and properties of phospholipase a from porcine pancreas" @default.
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- W2054184685 doi "https://doi.org/10.1016/0005-2744(68)90248-9" @default.
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