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Rapid purification of dipeptidyl peptidase IV from rat liver plasma membrane.

作者信息

Hartel S, Hanski C, Kreisel W, Hoffmann C, Mauck J, Reutter W

出版信息

Biochim Biophys Acta. 1987 Jun 22;924(3):543-7. doi: 10.1016/0304-4165(87)90170-x.

DOI:10.1016/0304-4165(87)90170-x
PMID:2885032
Abstract

Dipeptidyl peptidase IV (EC 3.4.14.5) was solubilized from rat liver plasma membranes with sulphobetaine 14 and purified by successive affinity chromatography on Con A-Sepharose, wheat germ lectin-Sepharose and arginine-Sepharose columns. The specific activity of the final preparation was 49.4 mumol Gly-Pro p-nitroanilide/min per mg protein, representing a 1098-fold purification of the homogenate. SDS-polyacrylamide gel electrophoresis of the arginine-Sepharose eluate showed a single protein band with a molecular weight of 105,000. The isoelectric point was determined to be 3.9 under non-denaturing conditions with sulphobetaine 14. The preparation was free of post-proline cleaving enzyme. The content of aminopeptidase M was 0.2% of the total protein.

摘要

相似文献

1
Rapid purification of dipeptidyl peptidase IV from rat liver plasma membrane.
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引用本文的文献

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A Fischer rat substrain deficient in dipeptidyl peptidase IV activity makes normal steady-state RNA levels and an altered protein. Use as a liver-cell transplantation model.一种二肽基肽酶IV活性缺陷的Fischer大鼠亚系能产生正常的稳态RNA水平和一种改变的蛋白质。用作肝细胞移植模型。
Biochem J. 1991 Feb 1;273 ( Pt 3)(Pt 3):497-502. doi: 10.1042/bj2730497.