title: Biochemical characterization of alkaline phosphatase from partly mineralized bovine enamel.
abstract: Alkaline phosphatase (AP) from partly mineralized bovine enamel was studied. The enzyme resembles alkaline phosphatases in other calcifying tissues. The Km was 0.46 mM; the phosphatase was strongly inhibited by 1 mM Levamisol or EDTA and it showed the same sensitivity towards heating as bone alkaline phosphatase. The inactivation caused by phosphate ions was approximately about 30%. In a zymogram, five isozymes of enamel alkaline phosphatase can be recognized. In a SDS-polyacrylamide gel a single band showing enzyme activity was visualized. This enzyme has an apparent molecular weight of 140,000.
authors.forename: D
authors.initials: D
authors.lastname: Moe
authors.forename: S
authors.initials: S
authors.lastname: Kirkeby
authors.forename: E
authors.initials: E
authors.lastname: Salling
mesh_terms: D000469:Alkaline Phosphatase / Q000032:analysis*; D000818:Animals; D002417:Cattle; D003743:Dental Enamel / Q000201:enzymology*; D007527:Isoenzymes / Q000032:analysis; D014074:Tooth Calcification
chemical_list: D007527:Isoenzymes; D000469:Alkaline Phosphatase