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• W2034370425 abstract "A pregastric lipase was purified from calf pharyngeal tissues. The purification procedure was based on chromatographies on octyl-Sepharose and lentil-lectin-Sepharose followed by gel filtration. The final preparation, with an overall recovery of 26% of activity, gave a single protein band on dodecyl sulfate/polyacrylamide gel electrophoresis with a Mr of 55000. The Mr on gel filtration was 44–48000. The discrepancy may be due to the fact that pregastric lipase is a glycoprotein containing ∼ 10% (w/w) of carbohydrate. The pI was around 7.0 and the enzyme protein is characterized by a high content of branched, aliphatic amino acid residues. The NH2-terminal amino acid sequence is: H2N-Phe-Leu/(Ile)-Gly-. Rabbit antibodies to the purified preparation detected only one component in the crude starting material in immuno-blotting experiments. Preincubation with antiserum resulted in loss of enzyme activity, showing that the antibodies were directed against the lipase." @default.
• W2034370425 created "2016-06-24" @default.
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• W2034370425 date "1985-04-01" @default.
• W2034370425 modified "2023-09-27" @default.
• W2034370425 title "Purification and molecular characterization of bovine pregastric lipase" @default.
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• W2034370425 doi "https://doi.org/10.1111/j.1432-1033.1985.tb08830.x" @default.
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