PMID: 36552Sep 1, 1977

Photooxidation of aspartate transaminase from chicken heart cytosol

Molekuliarnaia biologiia
A V AzarianIu M Torchinskiĭ

Abstract

Rose-bengal-sensitized photooxidation of aspartate transaminase from chicken heart cytosol results in a loss of enzymatic activity which follow first order kinetics down to 70--75% inactivation. 0.9 Histidine, 0.9 tryptophane residues and 1.5 SH groups per enzyme subunit were found to be modified in the photooxidized transaminase, which retained 26% residual activity. Photodestruction of the coenzyme was about 16%. The rate of enzyme photoinactivation is constant in the pH range 6--8, and drastically decreases with lowering pH from 6 to 4. alpha-Ketoglutarate partially protects the holoenzyme from inactivation. The apoenzyme undergoes photoinactivation at a rate almost twice as rapid as the holoenzyme. Photooxidized apotransaminase retains affinity to pyridoxal phosphate and binds as much coenzyme as the native apoenzyme. Photooxidation induces no significant alterations in the circular dichroism pattern of the enzyme in the 200 to 240 nm range. However, positive circular dichroism is markedly increased in the absorption bands of aromatic amino acids (260--300 nm). The affinity of photooxidized holoenzyme for glutarate and alpha-methyl aspartate is greatly decreased. On the other hand, photooxidized enzyme retains its ability t...Continue Reading

Related Concepts

Apoenzymes
Histidine
Aspartate
Amino Acids, I.V. solution additive
Alpha Ketoglutarate
Macromolecular Alteration
Myocardium
Pyridoxal Phosphate
Abufne
Aspartate Transaminase

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