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 K(M), whereas enzymes A1 and A2 had
low K(m). The enzymes A1 and A2 bound to antibodies raised against prostatic acid phosphatase,
whereas the enzymes B and C did not.