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- W2056344894 abstract "Summary Some of the acid phosphatase isozymes of bovine leucocytes and plasma have been separated and partly characterized. About 80% of the phosphatase activity of leucocytes at pH 4·9 was particle-bound and about 8% was extractable with Amberlite CG-50 ion exchange resin. This extractable enzyme existed as a single electrophoretic component with a mol. wt of about 42000 and with optimum activity at pH 5·8. K m for p -nitrophenyl phosphate was 1·6 mM at pH 5·8 and 0·4 mM at pH 4·9. At pH 5·8 orthophosphate (K 1 = 1·5 mM) and pyrophosphate (K i = 4·1 mM) were competitive inhibitors. The enzyme was also strongly inhibited by F − , Al 3+ , IO 4 − and S 2 0 3 2− . The enzyme which was not extractable with Amberlite was very heterogeneous with respect to molecular weight. At the pH optimum (4·9), K m for p -nitrophenyl phosphate was 0·4 mM and orthophosphate (K 1 = 2·3 mM) and pyrophosphate (K 1 = 2·1 mM) were competitive inhibitors. Other inhibitors included F − , Al 3+ , Hg 2+ , IO 4 − and tartrate. The enzyme extracted from plasma by Amberlite CG-50 treatment had properties similar to that extracted from leucocytes. Normal bovine milk contained a single acid phosphatase, but milk from cows with mastitis showed 3 electrophoretic isozyme bands, one being the same as in normal milk; the 2 additional bands were of leucocyte origin." @default.
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- W2056344894 date "1975-10-01" @default.
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- W2056344894 title "The acid phosphatases of bovine leucocytes, plasma and the milk of healthy and mastitic cows" @default.
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- W2056344894 doi "https://doi.org/10.1017/s0022029900015430" @default.
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