PMID: 36163Apr 12, 1979

Chemical and physical properties of the carboxypeptidase Y-inhibitor from Baker's yeast

Biochimica Et Biophysica Acta
H MaternH Holzer


The purification as well as some characteristics of the carboxypeptidase Y-inhibitor from baker's yeast have been described in a previous report (Matern, H., Hoffmann, M. and Holzer, H. (1974) Proc. Natl. Acad. Sci. U.S. 71, 4874-4878). In this paper, chemical and physical properties of the purified inhibitor are presented. The molecular weight was estimated at 23 400--24 000 and appears to be a monomeric unit. Amino acid analysis and carbohydrate studies are given, showing the existence of three disulfide bonds and one sulfhydryl group per molecule and the absence of carbohydrate residues. The N-terminal amino acid is blocked by an acetyl group. The C-terminal amino acid is lysine. The isoelectric point (pI) is 6.6 and the inhibitor-enzyme complex is stable (at 25 degrees C) betwen pH 5 and 9. The apparent Ki value was calculated as 2.5.10(-9)M.


Sep 1, 1973·Analytical Biochemistry·S C Kuo, E S Younathan
Oct 23, 1974·Biochemical and Biophysical Research Communications·J F LenneyJ Meyer
Oct 8, 1974·Biochemical and Biophysical Research Communications·H MaternH Holzer
Dec 1, 1974·Proceedings of the National Academy of Sciences of the United States of America·H MaternH Holzer
Feb 20, 1967·Archiv für Mikrobiologie·P Matile, A Wiemken
Jan 1, 1969·Archives of Biochemistry and Biophysics·J F Lenney, J M Dalbec
May 1, 1959·Archives of Biochemistry and Biophysics·G L ELLMAN
Mar 1, 1964·Biochemistry·D A YPHANTIS
Sep 8, 2005·Journal of Clinical Microbiology·Susanna K P LauKwok-Yung Yuen

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Enzyme Inhibitors
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