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牛蛙半胱氨酸蛋白酶抑制剂的纯化与鉴定

Purification and characterization of inhibitor against the cysteine proteinase of Rana catesbeiana.

作者信息

Fujita S, Horiuchi S

机构信息

Life Science Institute, Sophia University, Tokyo, Japan.

出版信息

Comp Biochem Physiol B. 1990;95(4):691-7. doi: 10.1016/0305-0491(90)90306-e.

Abstract
  1. Inhibitors of cysteine proteinase were found in tadpole tail of metamorphosing bullfrog. 2. One of the inhibitors was purified by affinity chromatography with CM-papain agarose, gel filtration with Superose 12 and ion exchange chromatography with Mono S. 3. The molecular weight of the inhibitor was 130,000-140,000 and the isoelectric point was pH 9.6. 4. The inhibitor had inhibitory effects on ficin, papain and tadpole tail cysteine proteinase. 5. The inhibitor is possibly involved in the regulation of muscle degradation in tail regression of metamorphosing tadpole.
摘要
  1. 在变态期牛蛙的蝌蚪尾巴中发现了半胱氨酸蛋白酶抑制剂。2. 其中一种抑制剂通过CM-木瓜蛋白酶琼脂糖亲和层析、Superose 12凝胶过滤和Mono S离子交换层析进行纯化。3. 该抑制剂的分子量为130,000 - 140,000,等电点为pH 9.6。4. 该抑制剂对无花果蛋白酶、木瓜蛋白酶和蝌蚪尾巴半胱氨酸蛋白酶有抑制作用。5. 该抑制剂可能参与了变态期蝌蚪尾巴退化过程中肌肉降解的调节。

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