Studies on the Proteinase-A Inhibitor I A 3 from Yeast

Studies on the Proteinase-A Inhibitor I A 3 from Yeast Hoppe-Seyler's Z. Physiol. Chem, B'-d. 357, S. 727 - 734, Mai 1976 Studies on the Proteinase-A Inhibitor IA from Yeast Ignacio NUNEZ de CASTRO and Helmut HOLZER Institut für Biochemie der Gesellschaft für Strahlen- und Umweltforschung und Biochemisches Institut der Universität Freiburg i.Br. (Received 9 February 1976) Summary: The purification and some properties of the two inhibitors l£ and 1^ of proteinase A from yeast have previously been described [Saheki et al. (1974)Eur. J. Biochem. 47, 325]. An improved method for the preparation of 1^ which is less time-consuming and leads to higher yields is presented. Based on amino acid analysis, 1^ contains 68 amino acids per molecule. The molecular weight was 7676. The inhibitor contained no proline, no arginine, no cysteine and no tryptophan, but did contain a large number of the polar amino acids glutamate + glutamine, aspartate + asparagine and lysine. Neither by dansylation nor by Edman degradation could an TV-terminal amino acid be detected. Changes in the circular dichroism upon transition from pH 6.9 to 3.0 suggest different tertiary structures at these pH values. Experiments on the kinetics of inhibition of proteinase A revealed an apparent K{ value of 5.5 10~8M for l£ and http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png hoppe-seyler's zeitschrift für physiologische chemie de Gruyter

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Publisher
de Gruyter
Copyright
Copyright © 1976 by the
ISSN
0018-4888
eISSN
1437-4315
DOI
10.1515/bchm2.1976.357.1.727
Publisher site
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Abstract

Hoppe-Seyler's Z. Physiol. Chem, B'-d. 357, S. 727 - 734, Mai 1976 Studies on the Proteinase-A Inhibitor IA from Yeast Ignacio NUNEZ de CASTRO and Helmut HOLZER Institut für Biochemie der Gesellschaft für Strahlen- und Umweltforschung und Biochemisches Institut der Universität Freiburg i.Br. (Received 9 February 1976) Summary: The purification and some properties of the two inhibitors l£ and 1^ of proteinase A from yeast have previously been described [Saheki et al. (1974)Eur. J. Biochem. 47, 325]. An improved method for the preparation of 1^ which is less time-consuming and leads to higher yields is presented. Based on amino acid analysis, 1^ contains 68 amino acids per molecule. The molecular weight was 7676. The inhibitor contained no proline, no arginine, no cysteine and no tryptophan, but did contain a large number of the polar amino acids glutamate + glutamine, aspartate + asparagine and lysine. Neither by dansylation nor by Edman degradation could an TV-terminal amino acid be detected. Changes in the circular dichroism upon transition from pH 6.9 to 3.0 suggest different tertiary structures at these pH values. Experiments on the kinetics of inhibition of proteinase A revealed an apparent K{ value of 5.5 10~8M for l£ and

Journal

hoppe-seyler's zeitschrift für physiologische chemiede Gruyter

Published: Jan 1, 1976

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