The activation of chymotrypsinogen isolation and identification of a peptide liberated during activation
- Creators
- Dreyer, William J.
- Neurath, Hans
Abstract
Reactions attending the conversion of precursors of proteolytic enzymes to the active form are distinguished by several features of unusual interest: (a) they are enzyme-catalyzed; (b) they are irreversible; (c) they involve the opening of a limited number of peptide bonds; (d) they provide an experimental system for the study of the final steps in formation of a biologically specific protein and of the relation of chemical structure to biological activity of proteins. In recent studies in this laboratory, including the present work, several intermediates formed during the activation of chymotrypsinogen have been recognized by a combination of methods. These have included electrophoresis, end-group analysis, enzymatic activity, peptide analysis, and sedimentation. As a result of the present experimental study, which dealt in particular with the nature of the peptide released during the rapid activation of chymotrypsinogen, it has been possible to identify the nature of the limited number of peptide bonds hydrolyzed during the activation process.
Additional Information
© 1955 Received for publication, May 12, 1955. Presented in part before the Forty-sixth annual meeting of the American Society of Biological Chemists at San Francisco, California, April 11-15, 1955. A preliminary report has been published. We are indebted to The Wilson Laboratories, Chicago, Illinois, for a crude protein precipitate, obtained from freshly collected beef pancreas glands, which served as starting material for the isolation of chymotrypsinogen and ɑ-chymotrypsin. Our thanks are due to Miss Elaine Cohen and Miss Anne Cederquist for performing the amino acid analysis and to Mr. Roger D. Wade for his assistance in electrophoretic measurements. This work has been supported by the United States Public Health Service, research grant C-2286, by contract No. Nonr-477-04 between the University of Washington and the Office of Naval Research, Department of the Navy, and by funds made available by the people of the State of Washington, Initiative 171.Additional details
- Eprint ID
- 50380
- Resolver ID
- CaltechAUTHORS:20141014-141602844
- C-2286
- U. S. Public Health Service
- Nonr-477-04
- U. S. Public Health Service
- University of Washington
- Office of Naval Research (ONR)
- Created
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2014-10-14Created from EPrint's datestamp field
- Updated
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2019-10-03Created from EPrint's last_modified field