Crystallization of recombinant human interleukin 1β

H.M. Einspahr; L.L. Clancy; Steven W. Muchmore; K. D. Watenpaugh; P. K. W. Harris; Donald B. Carter; K. A. Curry; Che-Shen C. Tomich; Anthony W. Yem; Martin R. Deibel; H. A. Zurcher-Neely; Robert L. Heinrikson

doi:https://doi.org/10.1016/0022-0248(88)90313-2

doi.org/10.1016/0022-0248(88)90313-2

Crystallization of recombinant human interleukin 1β

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..., Robert L. Heinrikson

45

Journal of Crystal Growth1.80

Volume: 90, Issue: 1-3, Pages: 180 - 187

Published: Jul 1, 1988

Abstract

The gene for the fully processed form of human interleukin 1β was cloned from SK-hep-1 hepatoma cellular RNA and expressed at high levels in E. coli. The protein produced in E. coli. was purified to homogeneity by standard chromatographic methods, including adsorption and desorption from Procion Red Sepharose, sizing on a Superose 12 FPLC column, and anion exchange chromatography on QAE Sepharose. The result is a biologically active protein,...

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Paper Details

Title

Crystallization of recombinant human interleukin 1β

DOI

doi.org/10.1016/0022-0248(88)90313-2

Published Date

Jul 1, 1988

Journal

Journal of Crystal Growth

Volume

90

Issue

1-3

Pages

180 - 187

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