[Solubilization of the AMP deaminase in the muscles of the teleost fish Scorpaena].
A considerable amount of AMP deaminase (AMPDA) in animal muscles is linked with myofibrils. This link is disturbed with growth of the ionic strength. A smooth increase of AMPDA solubilization has been showed in experiments with rabbit muscles when KCl concentration grew from 0 to 500 mM. Earlier we showed at trout muscles that an increase in KCl concentration from 0 to 200 mM in the homogenization medium induced growth of the bound enzyme portion followed by its decrease at the range of KCl concentrations 300-500 mM. Similar results were obtained in experiments with the sea scorpion muscles, which shows specific character of AMPDA interaction with myofibrils in teleost fish muscles. Comparison of the pH influence on AMPDA extraction from Scorpaena and rabbit muscles supported the idea on the specific character of this enzyme binding in the teleost muscles.
Smirnova
Iu D
IuD
Lushchak
V I
VI
D000659:AMP Deaminase / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D005399:Fishes / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D009132:Muscles / Q000201:enzymology*; D009210:Myofibrils / Q000201:enzymology; D012995:Solubility; D013056:Spectrophotometry, Ultraviolet
D000659:AMP Deaminase