Further Investigation of the Reducibility of Lyophilized Catalase
Author:
Affiliation:
1. Department of Biochemistry, School of Medicine and Dentistry, University of Rochester, Rochester, New York
Publisher
American Association for the Advancement of Science (AAAS)
Subject
Multidisciplinary
Reference4 articles.
1. DOUNCE, A.L., SCIENCE 97: 21 (1943).
2. KEILIN, D, PROPERTIES OF AZIDE-CATALASE, BIOCHEMICAL JOURNAL 39: 148 (1945).
3. SUMNER, J.B., The chemical nature of catalase, ADVANCES IN ENZYMOLOGY AND RELATED SUBJECTS OF BIOCHEMISTRY 1: 163 (1941).
4. VONEULER, H, Concerning catalase. I., JUSTUS LIEBIGS ANNALEN DER CHEMIE 452: 158 (1927).
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1. Electron spin resonance study of the role of NO . catalase in the activation of guanylate cyclase by NaN3 and NH2OH. Modulation of enzyme responses by heme proteins and their nitrosyl derivatives.;Journal of Biological Chemistry;1979-10
2. Fluoride and formate interaction with liver and erythrocyte catalases as revealed by solvent-proton magnetic relaxation;Biochemistry;1977-12-13
3. A study of the interaction of natural polymers — surfactants I. International of catalase (EC 1.11.1.6) with ionic surfactants;Colloid and Polymer Science;1976-01
4. Catalase: Physical and chemical properties, mechanism of catalysis, and physiological role.;Physiological Reviews;1970-07
5. Nature of the change produced in catalase by lyophilization;Archives of Biochemistry and Biophysics;1967-06
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