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Distinct glutathione-dependent enzyme activities and a verapamil-sensitive binding of xenobiotics in a fresh-water mussel Anodonta cygnea (CROSBI ID 124383)

Prilog u časopisu | izvorni znanstveni rad | međunarodna recenzija

Kurelec, Branko ; Pivčević, Branka Distinct glutathione-dependent enzyme activities and a verapamil-sensitive binding of xenobiotics in a fresh-water mussel Anodonta cygnea // Biochemical and biophysical research communications, 164 (1989), 2; 934-940. doi: 10.1016/0006-291X(89)91548-9

Podaci o odgovornosti

Kurelec, Branko ; Pivčević, Branka

engleski

Distinct glutathione-dependent enzyme activities and a verapamil-sensitive binding of xenobiotics in a fresh-water mussel Anodonta cygnea

A fresh-water mussel Anodonta cygnea, an aquatic invertebrate resistant to pollution, possesses an inherent high potential to bind 2-acetylaminofluorene onto membrane vesicles. This binding is saturable and trypsin- and verapamil- sensitive. Simultaneously, this mussel reveals a relatively high inherent activity of glutathione-dependent enzyme activities with a distinct spectrum of substrate affinities. Both these activities are similar to the elements of the molecular mechanism involved in the acquired multi-drug resistance phenomenon described in tumour cell-lines. The recognition that in organisms exposed to polluted waters a multi-xenobiotic resistance mechanism may be involved is essential for understanding both the biological impact of pollution and the development of methods for rational risk assessment in regulatory policy.

GSH ; glutathione ; GST ; glutathione transferase ; CDNB ; 1-chloro-2 ; 4-dinitro-benzene ; AAF ; 2-acetylaminofluorene ; MDR ; multi-drug resistance

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Podaci o izdanju

164 (2)

1989.

934-940

objavljeno

0006-291X

1090-2104

10.1016/0006-291X(89)91548-9

Povezanost rada

Biologija

Poveznice
Indeksiranost