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• W2000666456 abstract "A high-affinity and specific binding site for mammalian group I phospholipase A2 (PLA2-I) was found on the membranes of bovine corpus luteum. Affinity labeling experiments revealed that PLA2-I binds to a single polypeptide with a mass of 190–200 kDa. The PLA2-I binding protein in the membranes was solubilized in an active form with n-octyl β-d-thioglucoside, and then purified approx. 16 000-fold. The purification procedures consisted of diethylaminoethyl-Sephacel chromatography, PLA2-I-affinity gel chromatography and gel-filtration high-performanceliquid chromatography on a TSKgel G3,000SWXL column. The final preparation migrated as a single molecular species of 190 kDa on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and identification of the 190 kDa protein as the PLA2-I binding protein was demonstrated by ligand blotting analysis. The purified protein possessed a binding capacity with high affinity and specificity for a mammalian mature type of PLA2-I. Treatment of the purified material with N-glycosidase F resulted in increased mobility of the protein on SDS-PAGE as well as considerable abolition of the PLA2-I binding activity, thus suggesting the requirement of the carbohydrate moiety of the PLA2-I binding protein for receptor-ligand interactions." @default.
• W2000666456 created "2016-06-24" @default.
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• W2000666456 date "1992-08-01" @default.
• W2000666456 modified "2023-09-23" @default.
• W2000666456 title "Purification and characterization of a high-affinity binding protein for pancreatic-type phospholipase A2" @default.
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• W2000666456 doi "https://doi.org/10.1016/0005-2760(92)90226-l" @default.
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