Furia A, Palmieri M, Libonati M
Biochim Biophys Acta. 1983 Dec 22;741(3):303-7. doi: 10.1016/0167-4781(83)90149-5.
Native bovine seminal ribonuclease is a dimeric protein, whose identical subunits (Mr 14500), linked through two disulfide bridges, can be dissociated by a selective reduction procedure. Evidence is presented that the synthesis in vitro, under reducing conditions, of bovine seminal RNAase, directed by polyadenylated RNA isolated from bull seminal vesicles (where the enzyme is synthesized in vivo), occurs in the form of a precursor, 18000-Da polypeptide. The precursor nature of this translation product was deduced by two criteria: (1) its specific immunoprecipitation with anti-bovine seminal RNAase antibodies; (2) its processing by dog pancreas microsomal membranes to produce a protein with a molecular weight similar to that of the subunit(s) of bovine seminal RNAase. Moreover, evidence is offered that the precursor polypeptide is able to form in vitro a dimeric molecule under conditions where no exogenous reducing agents were added.
天然牛精浆核糖核酸酶是一种二聚体蛋白，其相同亚基（Mr 14500）通过两个二硫键相连，可通过选择性还原程序解离。有证据表明，在还原条件下，由从公牛精囊（该酶在体内合成的部位）分离的聚腺苷酸化RNA指导，体外合成牛精浆核糖核酸酶时，是以一种18000道尔顿多肽的前体形式出现的。这种翻译产物的前体性质是通过两个标准推断出来的：（1）用抗牛精浆核糖核酸酶抗体对其进行特异性免疫沉淀；（2）它被狗胰腺微粒体膜加工后产生一种分子量与牛精浆核糖核酸酶亚基相似的蛋白质。此外，有证据表明，在不添加外源还原剂的条件下，前体多肽能够在体外形成二聚体分子。
