The alkaline phosphatase of beef, horse, pig and sheep brain have been purified. In each case, the alkaline phosphatase activity can be separated into two or three components by DEAE-cellulose chromatography and by electrophoresis. Although the properties of these enzyme fractions are very similar, there are sufficient differences to identify each species.Furthermore two of the three components separated in sheep brain differ in their Michaelis constants using beta-glycerophosphate as substrate, whereas the two pig brain components are not different in this respect. This supports the view of two alkaline phosphatase isoenzymes in sheep brain.
Brunel
C
C
Laboratoire de Chimie biologique, Faculté des Sciences, 34 -, Montpellier, France
Cathala
G
G