Immunochemical Studies of Human Placental‐Type Variants of Alkaline Phosphatase

Publisher Website
Google Scholar
Abstract
Hyperimmune antisera raised against the rare FD and SD phenotypes of human placental alkaline phosphatase and the related cancer-associated Nagao isoenzyme were exhaustively absorbed with the common SS and FF phenotype enzymes conjugated to Sepharose. The antibodies so obtained had 1 of 3 specificities, determined by testing all the common phenotypes of placental alkaline phosphatase, the rare FD, SD and S-17 phenotypes, and 5 samples of purified cancer patient enzymes: (I) antibodies reactive with the S, D and I variant enzymes but not with the F, 17 or Nagao enzymes; (II) antibodies reactive with F, 17 and Nagao enzymes but not with S, D and I variant enzymes; and (III) antibodies reactive with D, 17 and Nagao enzymes and not with S, F or I variant enzymes. Based on these data, and on the information obtained from biochemical characterization, it is argued that the Nagao isoenzyme and the D-variant are closely related but distinct enzymes. A hypothetical scheme is proposed for the divergence of these 2 enzymes from a common ancestral gene product. In this scheme, an ancestral gene duplication resulted in 2 isoenzymes, one of which is completely specific to the placenta and one of which (the Nagao isoenzyme) has an unknown normal tissue localization but is found in some cases of cancer. The term syn-placental is used to describe this latter isoenzyme, reflecting its close structural relationship to the placental isoenzyme.