Details

Autor(en) / Beteiligte

• Waheed, A
• Laidler, P M
• Wo, Yu-Yuan P
• Van Etten, RL

Titel

Purification and physicochemical characterization of a human placental acid phosphatase possessing phosphotyrosyl protein phosphatase activity

Ist Teil von

• Biochemistry (Easton), 1984-01, Vol.27 (12), p.4265-4273

Erscheinungsjahr

1984

Quelle

Alma/SFX Local Collection

Beschreibungen/Notizen

• A 17-kilodalton (kDa) human placental acid phosphatase was purified 21,400-fold to homogeneity. The enzyme has an isoelectric point of pH 7.2 and a specific activity of 106 mu mol min super(-1) mg super(-1) using p-nitrophenyl phosphate as a substrate at pH 5 and 37 degree C. This placental acid phosphatase showed activity toward phosphotyrosine and toward phosphotyrosyl proteins. Enzyme activity was also inhibited by DNA, but RNA was not inhibitory. It is a hydrophobic nonglycoprotein containing approximately 20% hydrophobic amino acids.