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• W2028014083 abstract "Two 67 kDa proteins adsorbed to membranes in the presence of Ca 2+ have been purified to homogeneity from pig lung using conventional procedures, followed by calcium‐dependent affinity chromatography on polyacrylamide‐immobilized phosphatidylserine. The two proteins were, respectively, excluded (67E) and retained (67R) on the column in the presence of Ca 2+ . On the basis of amino acid composition and isoelectric point, 67R was identified as 67 kDa calelectrin/calcimedin, whereas 67E could be differentiated from albumin, calregulin, 67 kDa fragment of protein kinase C and surfactant‐associated proteins. Only 67R was slightly phosphorylated by protein kinase C, reacted with an antibody raised against 32.5 kDa endonexin and inhibited pig pancreas phospholipase A 2 in a way similar to that of lipocortin or endonexin. These data bring further support to the view that inhibition of phospholiphase A 2 by lipocortin or other related proteins involves interaction with the lipid/water interface. They also provide evidence for a new kind of Ca 2+ ‐binding protein (67E), whose role still remains to be determined." @default.
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• W2028014083 date "1987-09-14" @default.
• W2028014083 modified "2023-10-07" @default.
• W2028014083 title "Isolation of two 67 kDa calcium-binding proteins from pig lung differing in affinity for phospholipids and in anti-phospholipase A₂activity" @default.
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• W2028014083 doi "https://doi.org/10.1016/0014-5793(87)80963-8" @default.
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