Fini C, Camici M, Minelli A, Floridi A, Ipata P L
Int J Biochem. 1986;18(8):683-9. doi: 10.1016/0020-711x(86)90390-3.
Both purified and membrane-bound 5'-nucleotidases (EC 3.1,3.5) from guinea pig skeletal muscle and bull seminal plasma are inhibited by Concanavalin A (Con A). 5'-Nucleotidase purified from skeletal muscle is inhibited by Con A by an apparent uncompetitive process (K'i = 160 nM), while the lectin inhibits the particulate enzyme by an apparent non-competitive process (Ki = K'i = 50 nM). 5'-Nucleotidase purified from bull seminal plasma is inhibited by Con A by an apparent non-competitive process (K'i = Ki = 270 nM), while the membrane-bound enzyme is subjected to a mixed type inhibition by the lectin (K'i greater than Ki; 30 and 14 nM, respectively). The enzyme purified from skeletal muscle exhibits a significant cooperativity in the interaction with Con A. The inhibition of bull seminal plasma particulate 5'-nucleotidase brought about by Con A is not completely reversed by addition of alpha-methyl-D-mannoside.
豚鼠骨骼肌和公牛精浆中的纯化型和膜结合型5'-核苷酸酶（EC 3.1,3.5）均受伴刀豆球蛋白A（Con A）抑制。从骨骼肌中纯化的5'-核苷酸酶受Con A抑制的过程表现为明显的非竞争性（K'i = 160 nM），而凝集素对颗粒酶的抑制则表现为明显的非竞争性（Ki = K'i = 50 nM）。从公牛精浆中纯化的5'-核苷酸酶受Con A抑制的过程表现为明显的非竞争性（K'i = Ki = 270 nM），而膜结合型酶则受到凝集素的混合型抑制（K'i大于Ki；分别为30和14 nM）。从骨骼肌中纯化的酶在与Con A相互作用时表现出显著的协同性。Con A对公牛精浆颗粒5'-核苷酸酶的抑制作用不会因添加α-甲基-D-甘露糖苷而完全逆转。
