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Fluorometric analysis of native, urea-denatured and refolded human prostatic acid phosphatase

✍ Scribed by Wlodzimierz S. Ostrowski; Radoslawa Kuciel; Fumio Tanaka; Kunio Yagi


Book ID
113269211
Publisher
Elsevier Science
Year
1993
Tongue
English
Weight
829 KB
Volume
1164
Category
Article
ISSN
0167-4838

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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