Partial purification and characterization of an alkaline phosphatase in Helix nemoralis and in Octopus vulgaris.
1. Alkaline phosphatase (AP) present in the liver of Helix nemoralis and of Octopus vulgaris; enzyme was purified by homogenization, ultracentrifugation, n-butanol treatment, acetone fractionation and Sephadex G-200 chromatography. 2. The two enzymes show a similar enzyme-substrate affinity, but differ in several properties (molecular weight, electrophoretic mobility, optimum pH, substrate inhibition); a possible correlation of them with different evolutionary adaptations is suggested. 3. Possible roles of AP in Mollusca are discussed.
D000469:Alkaline Phosphatase / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D006372:Helix, Snails / Q000201:enzymology*; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D049831:Octopodiformes / Q000201:enzymology*; D013045:Species Specificity
D000469:Alkaline Phosphatase