Title : Purification and properties of a membrane-bound phospholipase A2 from rat ascites hepatoma 108A cells.

Pub. Date : 1980 Mar

PMID : 7390973






1 Functional Relationships(s)
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1 A phospholipase A2 bound tightly to the particulate fractions of rat ascites hepatoma cells was purified approximately 13,000-fold with a reasonably high yield (34%) by extraction with sodium cholate, ammonium sulfate fractionation, solubilization with sodium dodecyl sulfate, column chromatographies on Sephadex G-150 in the presence of sodium dodecyl sulfate, and on DEAE-cellulose and CM-cellulose in the presence of Triton X-100. Sodium Cholate phospholipase A2 group IB Rattus norvegicus