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The adaptation of mussels Crenomytilus grayanus to cadmium accumulation result in alterations in organization of microsomal enzyme-membrane complex (non-specific phosphatase)
Zakhartsev, M.V.; Chelomin, V.P.; Belcheva, N.N. (2000). The adaptation of mussels Crenomytilus grayanus to cadmium accumulation result in alterations in organization of microsomal enzyme-membrane complex (non-specific phosphatase). Aquat. Toxicol. 50(1-2): 39-49. dx.doi.org/10.1016/S0166-445X(99)00097-1
In: Aquatic Toxicology. Elsevier Science: Tokyo; New York; London; Amsterdam. ISSN 0166-445X, more
Peer reviewed article  

Available in Authors 
    VLIZ: Open Repository 280182 [ OMA ]

Keyword
    Marine
Author keywords
    in vivo; in vitro; non-specific phosphatase; membrane-bound enzyme;

Authors  Top 
  • Zakhartsev, M.V., more
  • Chelomin, V.P.
  • Belcheva, N.N.

Abstract
    The kinetic parameters (Vm, Km, and slope) of membrane-bound microsomal non-specific phosphatase NPase, with G6P as the substrate) from the digestive gland of unexposed and cadmium adapted (45 days for 100 µg Cd2+/l) mussels were investigated. In vivo and in vitro approaches were used. Adaptation of mussels (Crenomytilus grayanus) to cadmium resulted in a 1.6-fold increase in NPase activity. Vm was increased by 1.6-fold, bat Km was the same in terms of enzyme kinetics. This indicates that the total concentration of the enzymes in the digestive gland increased. Cd2+ (1 mM) did not significantly alter the activity of the membrane-bound enzyme in vitro both for unexposed and For cadmium adapted mussels, meaning that cadmium ions are not a direct inhibitor of the membrane-bound enzyme in this concentration. The microsomal NPase activity in both unexposed and cadmium adapted mussels was inhibited by in vitro solubilization of microsomes with non-ionic detergent (Triton X100, 0.01%). This inhibition was uncompetitive for microsomes of unexposed mussels (Km decreased 3.1-fold). The most drastic events were observed in cadmium adapted mussels, where inhibition was mixed (Km decreased 7.2-fold). The simultaneous actions of detergent and cadmium ions did not alter NPase activity significantly in comparison with action of the detergent alone. The differences in the types and the extents of inhibition of the enzymes activity by membrane disordering agent (Triton X100) indicated that the enzyme membrane complex (NPase) has been altered as a result of adaptation of mussels to cadmium accumulation. We conclude that the mussels produced a new Enzyme-membrane complex, with the same Km as the previous complex, but with other detergent sensitivity and greater amounts. Thus, the adaptation capacity of this enzyme is reduced as result of adaptation of mussels to cadmium accumulation.

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