Rosales-Encina J L, Campos-Salazar M S, Rojkind Matluk M
Departamento de Patología Experimental, CINVESTAV-IPN, México, DF.
Arch Med Res. 1992;23(2):109-13.
Three main collagen binding proteins from trophozoites of E. histolytica have been isolated: 105 kDa, 56 kDa and 30 kDa. They display a type I collagenolytic activity. The enzyme behaves as a mammalian collagenase regarding to its activity, collagen degradation products and inhibitors. Antibodies against affinity-purified molecules inhibit the binding of trophozoites to collagen substrates. Indirect evidence suggests that the 30 kDa molecule is the putative collagen receptor. These surface molecules may be necessary for attachment and migration of the parasite into solid tissue.
105 kDa、56 kDa和30 kDa。它们具有I型胶原酶活性。就其活性、胶原降解产物和抑制剂而言，该酶表现得如同哺乳动物胶原酶。针对亲和纯化分子的抗体可抑制滋养体与胶原底物的结合。间接证据表明，30 kDa分子是假定的胶原受体。这些表面分子可能是寄生虫附着并迁移至实体组织所必需的。
