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Purification and properties of the adenosine deaminase from the midgut gland of a marine bivalved mollusc, Atrina spp.
Metadata
JournalComp. Biochem. Physiol., BNot FoundDate
1977
Type
Research Support, U.S. Gov't, P.H.S.
Research Support, U.S. Gov't, Non-P.H.S.
Journal Article
Volume
1977 / 58 : 357-64
Author
Aikawa T 1, Umemori-Aikawa Y , Fisher JR
Affiliation

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Doi
PMIDMESH
Adenosine Deaminase
Animals
Chromatography, Gel
Hydrogen-Ion Concentration
Kinetics
Magnesium
Manganese
Mollusca
Nucleoside Deaminases
Temperature
Abstract
1. The adenosine deaminase has an approximate molecular weight of 130,000-140,000 and the composition of two polypeptide units (mol. wt about 68,000) is suggested, by means of SDS disc electrophoresis. 2. Both the alpha (Vm/Km) and beta (Vm) parameters were varied with pH and temperature. RSS (relative substrate specificity) adenosine and deoxyadenosine values for alpha and beta were 1.2 and 1.1, respectively. 3. Adenine, 2'-, 3', 5'-AMP, 5'-deoxyAMP, ADP and ATP were not deaminated by the enzyme. 4. Inhibition by Mg2+ was found in reaction with adenosine at pH 8 but not with deoxyadenosine at the same pH. Mn2+, which did not affect the reaction rate at pH 4 and 5, showed competitive inhibitory effects at pH 6, 7 and 8.
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Comp. Biochem. Physiol., BComparative biochemistry and physiology. B, Comparative biochemistry
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