Abstract
A mutant erythrocyte B type carbonic anhydrase has been found in a Caucasian. The isozyme was isolated in crystalline form and various of its properties were explored. It was similar in electrophoretic properties to the P isozyme previously found in pooled erythrocytes of normal individuals. It differs from the normal B and P isozymes in that 1 aspartic acid residue is substituted by valine. This variation was localized to a chymotryptic undecapeptide whose sequence was determined.
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