Acid phosphatases of the human placenta, characterization and immunological comparison with prostatic acid phosphatase.
Four different acid phosphatases, denoted A1, A2, B and C, were separated from human placental homogenates. The enzymes A1, A2 and B were separated from enzyme C by binding to concanavalin A-Sepharose. Although the A1, A2 and B enzymes were all strongly inhibited by L-tartrate, only the A1 enzyme bound by affinity chromatography to L-tartrate-Sepharose. The A2 and B enzymes were separated on DEAE-cellulose. A1, A2 and B had molecular weights about 95,000. Enzyme B had high KM, whereas enzymes A1 and A2 had low KM. The enzymes A1 and A2 bound to antibodies raised against prostatic acid phosphatase, whereas the enzymes B and C did not.
D000135:Acid Phosphatase / Q000032:analysis* / Q000276:immunology / Q000302:isolation & purification; D005260:Female; D006801:Humans; D007700:Kinetics; D008297:Male; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy; D011467:Prostate / Q000201:enzymology*; D013644:Tartrates
D013644:Tartrates; D000135:Acid Phosphatase