title: Separation and partial purification of acid phosphates of the enamel organ of rat molars.
abstract: At least two types of acid phosphatases with markedly different properties were separated from the enamel organ of rat molar tooth buds. One enzyme (A) bound weakly to the CM-cellulose column and was eluted with a combined linear salt and pH gradient; another enzyme (B) bound strongly to the column and was eluted with a second linear salt gradient at constant pH. Enzyme A was identified as a phosphomonoester hydrolase (3.1.3.2) similar to the lysosomal enzyme of soft tissues and the tartrate-sensitive enzyme of bone. Enzyme B did not hydrolyse aliphatic monophosphate ester substrates but, like enzyme A, it did split the aryl monophosphate ester substrate, para-nitrophenylphosphate, as well as the phosphate esters of casein and the acid anhydride substrates, ATP and inorganic pyrophosphate. This enzyme is similar to the low molecular weight tartrate-resistant acid phosphatases of bone and soft tissues.
mesh_terms: D000135:Acid Phosphatase / Q000302:isolation & purification* / Q000378:metabolism; D000818:Animals; D002845:Chromatography; D004658:Enamel Organ / Q000201:enzymology*; D008963:Molar / Q000201:enzymology; D051381:Rats; D011919:Rats, Inbred Strains; D014083:Tooth Germ / Q000201:enzymology*
chemical_list: D000135:Acid Phosphatase