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Article

Inhibitory activity and conformational transition of alpha 1-proteinase inhibitor variants.

European journal of biochemistry - 18 Dec 1991

Schulze A J, Huber R, Degryse E, Speck D, Bischoff R

Abstract excerpt

Several variants of alpha 1-proteinase inhibitor (alpha 1-PI) were investigated by spectroscopic methods and characterized according to their inhibitory activity. Replacement of Thr345 (P14) with Arg in alpha 1-PI containing an Arg residue in position 358 (yielding [Thr345----Arg, Met358----Arg]alpha 1-PI) results in complete loss of its inhibitory activity against human alpha-thrombin; whereas an exchange of...

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PMID: 1765073
DOI: 10.1111/j.1432-1033.1991.tb16483.x

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