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牛脾二肽酶(Dipeptidyl Aminopeptidase Ⅰ,简称DAP-Ⅰ)是一种蛋白酶,它能从多肽链的自由N-末端连续切下二肽,直到遇到精氨酸、赖氨酸或脯氨酸为止,故可用于多肽的结构测定。但是,至今DAP-Ⅰ制剂仍是不均一的并且不能长期保存。 本文报导了用亲和层析法从DAP-Ⅰ中除去其它两个二肽酶——组织羧肽酶C(Cathe-ptic Carboxypeptidase C)和丝氨酰蛋氨酸二肽酶(Ser-Met Dipeptidase)等杂蛋白,并报导了将DAP-Ⅰ制成汞盐,在低温下长期保存的方法。
Dipeptidyl Aminopeptidase I (DAP-I) is a protease that cleaves dipeptides continuously from the free N-terminus of polypeptide chains until it encounters arginine, lysine, or proline So far, it can be used for structural determination of the polypeptide. However, to date, DAP-I preparations are still not homogeneous and can not be preserved for a long time. This article reports the removal of two other dipeptidases, Cathe-ptic Carboxypeptidase C and Ser-Met Dipeptidase, from DAP-I by affinity chromatography Hybrid proteins, and reported the DAP-Ⅰ made mercury salts, long-term preservation at low temperatures.