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Isolation of serine phosphate from the active site of human prostatic acid phosphatase; Inhibition of the enzyme by DFP

✍ Scribed by Hanna Greenberg; David Nachmansohn

Book ID
118847930
Publisher
Elsevier Science
Year
1962
Tongue
English
Weight
161 KB
Volume
7
Category
Article
ISSN
0006-291X

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The enzyme human prostatic acid phosphatase is normally metal-free in its native state but can be stoichiometrically inactivated with cupric acetate. Direct structural evidence is reported for the participation of two histidine residues in the Cu 2/ binding site. X-Ray absorption fine structure spec