Human liver alkaline phosphatase, purification and partial sequencing: Homology with the placental isozyme

Abstract

Human liver alkaline phosphatase (AP) has been purified to homogeneity. The enzyme has a molecular weight of 150,000 in its native state and consists of two identical subunits of M r 75,000. After treatment with endoglycosidase F the molecular weight is reduced to 50,000 indicating a high degree of glycosylation. The amino-terminal sequence up to 22 residues was found to be LeuValProGluLysGluLysAspProLys Tyr(Ala)ArgAspGlnAlaGln?ThrLeuLysTyr. The amino-terminal portions of human and bovine liver AP are identical. The amino termini of the human liver and human placental AP isozymes have appreciable homology. Conformationally the amino termini are very similar.