Studies on the separate isozymes of red cell acid phosphatase phenotypes A and B

Abstract

SUMMARY Comparisons were made of some of the properties of the isozymes of types A and B red cell acid phosphatase. In each case, the more anodal isozyme had a higher pH optimum and a lower K m for ^‐nitrophenyl phosphate. Thermostability tests indicated that this isozyme was also the least stable in both types. Evidence is also presented which suggests that the two isozymes within one type are interconvertible.