作者: Giampietro Ramponi , Giampaolo Manao , Guido Camici , Gianni Cappugi , Marco Ruggiero
DOI: 10.1016/0014-5793(89)80778-1
关键词:
摘要: In this paper we demonstrate that the cytosolic low-M~ acid phosphatase purified from bovine liver has phosphotyrosine protein acitivity on aep-autophosphorylated epidermal growth factor (EGF) receptor. This activity was significantly inhibited by orthovanadate and p-hydroxymercuribenzoate; latter result indicates free sulfhydryl groups are required for activity. The enzyme active in a broad pH range, with maximum between 5.5 7.5. apparent Km 32P-EGF receptor dephosphorylation 4 riM. appeared to be specific it dephosphorylated autophosphorylated EGF L-phosphotyrosine, but not a2P-Ser-casein, L-phosphoserine or L-phosphothreonine. These data suggest low-Mr might play regulatory role receptor-dependent transmembrane signalling. Acid phosphatase; Epidermal receptor; Phosphotyrosine