Substrate-dependent apparent activation energies of the adenosine deaminases from bivalved molluscs
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,General Medicine,Physiology,Biochemistry
Reference12 articles.
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2. Kinetic properties of adenosine deaminase in mixed aqueous solvents;Bolen;Biochemistry,1969
3. Steady state kinetics;Cleland,1970
4. True and apparent activation energies of enzymic reactions;Gibson;Biochim. biophys. Acta,1953
5. Enzymes;Haldane,1930
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1. Adenosine deaminase in the adductor muscle of the scallop, Patinopecten yessoensis;Comparative Biochemistry and Physiology Part B: Comparative Biochemistry;1991-01
2. Kinetic characteristics and binding process of substrate analogs to the adenosine deaminase in the marine mussel, mytilus edulis;Comparative Biochemistry and Physiology Part B: Comparative Biochemistry;1987-01
3. Adenosine deaminase in the marine mussel, Mytilus edulis: Purification, characterization and inhibition by a substrate analog, coformycin;Comparative Biochemistry and Physiology Part B: Comparative Biochemistry;1984-01
4. Amino Acid Metabolism in Molluscs11This paper was written during the tenure of a National Science Foundation Grant-in-Aid (PCM-80–22606) and represents contribution number 156 from the Tallahassee, Sopchoppy, and Gulf Coast Marine Biological Association.;Metabolic Biochemistry and Molecular Biomechanics;1983
5. Concentrations of lactate and pyruvate and temperature effects on lactate dehydrogenase activity in the tissues of the big brown bat (Eptesicus fuscus) during arousal from hibernation;Comparative Biochemistry and Physiology Part B: Comparative Biochemistry;1982-01
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