Isozymes of bovine intestinal alkaline phosphatase

Alkaline phosphatases from calf and bovine small intestines have been isolated in homogeneous form from both mucosa and luminal contents. The detergent-solubilized calf enzyme resolves into two peaks of activity, C-1 and C-2, on chromatofocusing. Only one of these activity peaks is present in the enzyme from the adult animal. Amino acid compositions, N-terminal sequences, and tryptic peptide maps show that C-1 and C-2 are isozymes of differing primary structure and that the adult form of the enzyme is identical to C-2. The developmentally controlled expression of the two isozymes reported here suggests a molecular basis for the previous indications that functional changes in intestinal alkaline phosphatase occur with tissue maturation. The sugar composition of the carbohydrate chains of these isozymes has been determined and enzymatic deglycosylation with endo-beta-N-acetylglucosaminidase-F indicates two N-linked and one or more O-linked glycoconjugates/monomer.