|
|
||||||||
American Journal of Clinical Nutrition, Vol 22, 1222-1239, Copyright © 1969 by The American Society for Clinical Nutrition, Inc.
1 From Biophysics Research Laboratory, Department of Biological Chemistry, Harvard Medical School, and the Division of Medical Biology, Peter Bent Brigham Hospital, Boston, Massachusetts
The modes of approach that serve as guidelines to the discovery, isolation, and characterization of metalloproteins and metalloenzymes are presented. Metalloenzymes offer unique features which allow an approach to the mechanism of enzyme action in a manner that differs qualitatively from that allowed in nonmetalloenzymes.
The study of zinc metalloenzymes has played a major role in the elucidation of these general principles. Bovine pancreatic carboxypeptidase, yeast and mammalian alcohol dehydrogenases, and E. coli alkaline phosphataseall zinc metalloenzymesnot only illustrate these features but also demonstrate the role that zinc contributes to generating their characteristic biologic activity.
The pertinence of these zinc-dependent biologic systems to physiologic processes and their implications towards definition and treatment of conditions arising in human disease are discussed.
This article has been cited by other articles:
![]() |
I. Mitchell, L. Brady, J. Black, M. Jamieson, J. Pollock, and R. Logan The acute phase response to cardiopulmonary bypass in children Perfusion, March 1, 1996; 11(2): 103 - 112. [Abstract] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |