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Calf Intestinal Alkaline Phosphatase I. Improved Isolation Method and Molar Composition of the Purified Phosphatase
Author(s) -
Portmann Plato,
Jörg Andreas,
Furrer Kurt,
Walker HansSepp,
Leuthard Peter,
Sudan JeanFrançois,
Perriard FrançOis,
Comment JeanFrançois,
Leva Geneviève,
Nell Jeanpierre
Publication year - 1982
Publication title -
helvetica chimica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.74
H-Index - 82
eISSN - 1522-2675
pISSN - 0018-019X
DOI - 10.1002/hlca.19820650836
Subject(s) - chemistry , alkaline phosphatase , acid phosphatase , phosphoric acid , chromatography , enzyme , composition (language) , zinc , phosphatase , molar , biochemistry , ultracentrifuge , polyacrylamide gel electrophoresis , organic chemistry , medicine , linguistics , philosophy , dentistry
A modified and improved method for isolation of calf intestinal alkaline phosphatase is described. By this method 300 to 400 mg of pure enzyme was prepared in a relatively short time. On the basis of the results of ultracentrifugation and of the free, polyacrylamide and immunoelectrophoresis the phosphatase obtained is found to be a homogenous glycoprotein, containing firmly bound zinc, magnesium and phosphoric acid. The molar composition of the enzyme and the catalytic activity were determined with different substrates and buffers.