小白鼠貯精囊分泌蛋白中蛋白?抑制因數的研究

Abstract

經鹽析法、column chromatography 小白鼠貯精囊液的 protease inhibitor 可被分離。此 inhibitor 為蛋白質，其分子量為 5500 dalton ，胺基酸組成及氮端前 24 個胺基酸已決定。這些結果與小白鼠的Ventral prostate的 MP 12 cDNA 所推演的蛋白質之結講十分相似。本研究還直接證明瞭 MP 12 Signal peptide 的 Cleavages site 為 23(ser)，24(Ala) 。所分離的 protease inhibitor抑制 trypsin 的能力與 soybean trypsin inhibitor 的能力幾乎一樣強。

The protease inhibitor in mouse seminal vesicle fluid was purified consecutively by salting out process and preparing by trypsin attached affinity column chromatography. The protease inhibitor is a protein with Mr of 5500 dalton. It's amino acid composition and the N-terminal 24 amino acid residues sequences were determined. These results indicated that the primary structures of the seminal vesicle protease inhibitors was probably the same as protease inhibitors in mouse ventral prostate. My results also demonstrated that the signal peptide's leavage site of MP 12 should be between 23 (Ser) and 24 (Ala). The protease inhibitor efficiently suppressed the activity of trypsin as strong as the soybean trypsin inhibitor.