Griger B, Frensdorff A, Kraicer P F
Immunology. 1974 Oct;27(4):729-38.
The native secretion of rat seminal vesicles was found to contain about 290 mg of protein/ml. The ionic strength of the secretion was low (33 millimho. cm). Some protein (about 13 per cent) precipitated shortly after collection. The soluble proteins were resolved by electrophoresis into four very basic and two minor acidic fractions. Three of the proteins were eluted from a Sephadex G-200 column at a position indicating a molecular weight much in excess of 150,000 daltons; the others were eluted at a position intermediate between IgG and bovine serum albumin (BSA) markers. Ten bands were resolved in polyacrylamide gel electrophoresis following dissociation of the soluble proteins into subunits. Eight of these had molecular weights ranging between 18,500 and 100,000 Daltons. Antisera raised in rabbits against seminal vesicle fluid (SVF) formed, in immunoelectrophoresis (IE) six precipitin bands with SVF. They did not react at all with rat serum proteins, nor did antiserum to rat serum proteins react with SVF. A small amount of rat serum proteins was, however, detected by radioimmunoassay in the insoluble fraction.
发现大鼠精囊的天然分泌物每毫升含有约290毫克蛋白质。分泌物的离子强度较低（33毫姆欧·厘米）。收集后不久，一些蛋白质（约13%）沉淀下来。可溶性蛋白质通过电泳分离为四个非常碱性和两个次要酸性组分。其中三种蛋白质从Sephadex G - 200柱上洗脱的位置表明分子量远超过150,000道尔顿；其他蛋白质在免疫球蛋白（IgG）和牛血清白蛋白（BSA）标记物之间的中间位置洗脱。可溶性蛋白质解离成亚基后，在聚丙烯酰胺凝胶电泳中分辨出十条带。其中八条的分子量在18,500至100,000道尔顿之间。用兔抗精囊液（SVF）血清在免疫电泳（IE）中与SVF形成六条沉淀带。它们与大鼠血清蛋白完全不反应，抗大鼠血清蛋白的血清也不与SVF反应。然而，通过放射免疫测定法在不溶性部分中检测到少量大鼠血清蛋白。
