Purification and properties of glutamate dehydrogenase from the mantle muscle of the squid,Loligo pealeii. Role of the enzyme in energy production from amino acids
✍ Scribed by Storey, Kenneth B. ;Fields, Jeremy H. A. ;Hochachka, Peter W.
- Publisher
- John Wiley and Sons
- Year
- 1978
- Tongue
- English
- Weight
- 619 KB
- Volume
- 205
- Category
- Article
- ISSN
- 0022-104X
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✦ Synopsis
Abstract
The activity of glutamate dehydrogenase was measured in the tissues of the squid, Loligo pealeii. The enzyme occurs in high activity in digestive pouch, systemic heart, and all muscle tissues.
Glutamate dehydrogenase from mantle muscle is located intra‐mitochondrially, has a molecular weight of 310,000, and is electrophoretically similar to the enzyme, from all other squid tissues.
The enzyme from mantle muscle was purified 40‐fold by elution from DEAE‐cellulose and used for kinetic studies. The enzyme is NAD^+^‐specific, activated by ADP, AMP, and leucine, and inhibited by GTP, GDP, ATP, and reaction products (in particular NADH).
Squid glutamate dehydrogenase shows an almost absolute dependence on ADP. The purified enzyme is activated over 100‐fold by saturating concentrations of ADP (K)~a~ = 0.75 mM). The pH optima are also altered significantly by ADP.
The enzyme appears to be kinetically adapted to favour glutamate oxidation in comparison to glutamate dehydrogenase from other sources. The evidence indicates that the primary role of glutamate dehydrogenase in squid mantle muscle is in regulating the catabolism of amino acids for energy production.