Abstract
As previously reported 5), human serum alkaline phosphatase (Alp) isozymes are separated into 5 isozyme bands on thin layer polyacrylamide gel electrophoresis. According to their anodal migration, they are numbered as Alp I, II, III, IV and 0, respectively. The results are:
Neuraminidase released neuraminic acids from the polysaccharide chains of Alp isozymes except one (Alp IV).
Anti Lewis b serum formed complexes with Alp IV, and it is supposed that fucose instead of neuraminic acid is the terminal sugar of Alp IV and that a part of endpolysaccharide chain of Alp IV has the same sugar sequence as that of blood type Lewis b substance.
Phytohemagglutinin formed complexes with Alp III and it suggests that a part of endpolysaccharide chain of Alp III has the same sugar sequence of polysaccharide which is required by the receptor sites of phytohemagglutinin.
These data suggest that the endpolysaccharide chains of Alp isozymes are different from each other and are controled by different modifying genes together with the structure genes.
