Reversible inactivation of acid phosphatase in human prostatic extracts in vitro
✍ Scribed by Henry J. Tagnon; Andrée Steens-Lievens
- Publisher
- John Wiley and Sons
- Year
- 1960
- Tongue
- English
- Weight
- 503 KB
- Volume
- 13
- Category
- Article
- ISSN
- 0008-543X
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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
The stimulated secretion of prostatic acid phosphatase (PAcP) has been known to be a hallmark of androgen action on human prostate epithelial cells for the last five decades. The molecular mechanism of androgen action on PAcP secretion, however, has remained mostly unknown. We investigated the molec