Abstract
Two electrophoretic variants of leucine aminopeptidase show direct association with two genetically controlled forms of alkaline phosphatase. Treatment of plasma with neuraminidase converted the faster-migrating form of both enzymes to slower-moving forms, but plasmas with slower-migrating forms were unaffected by this treatment. The two forms of the enzymes may be due to the presence or absence of a single gene controlling the attachment of sialic acid to the enzyme molecules.