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Affinity purification of renal dipeptidase solubilized with detergent

✍ Scribed by Michael J.M. Hitchcock; Cathy A. Farrell; Susan Huybensz; Bing-Yuh Luh; David J. Phelps

Publisher: Elsevier Science
Year: 1987
Tongue: English
Weight: 860 KB
Volume: 163
Category: Article
ISSN: 0003-2697
DOI: 10.1016/0003-2697(87)90116-3

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✦ Synopsis

A new method is described for purification of the dehydropeptidase I enzyme, renal dipeptidase (EC 3.4.13. I I). The six steps used are homogenization ofthe tissue, extraction with Triton X-100, sedimentation of insoluble material, and ion-exchange, size-exclusion, and affinity chromatographies. The use of Triton X-100 to solubilize the enzyme is a major advantage over the previously described procedure using n-butanol and results in both improvements in yield and interexperimental consistency. Also, the affinity column method we have employed results in higher recovery of active enzyme at the final step and a product which is apparently homogeneous. The method has general utility for this class of enzymes.

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