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Purification and some properties of a Mg2+-activated acid phosphatase from rat testis

✍ Scribed by F. Panara; A. Angiolillo; I. Di Rosa; A. Fagotti; S. Contenti; F. Simoncelli; S. Lorvik; R. Pascolini

Publisher
Elsevier Science
Year
1994
Tongue
English
Weight
565 KB
Volume
26
Category
Article
ISSN
0020-711X

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An acid phosphatase from derepressed cells of the yeast form of Yarrowia lipolyrica was purified 176-fold by ammonium sulfate precipitation, chromatography on DEAE-Sephacel and gel filtration in Biogel A 5-M. The enzyme is a glycoprotein with a sugar content of 60%. The MICHAELIS constant of the enz