Glutathione transferase isoenzymes from frog (Xenopus laevis) liver and embryo

被引:17
作者
Angelucci, S
Sacchetta, P
De Luca, A
Moio, P
Amicarelli, F
Di Ilio, C
机构
[1] Univ G Dannumzio, Dipartimento Sci Biomed, I-66013 Chieti, Italy
[2] Univ Aquila, Dipartimento Biol Base & Applicata, I-67100 Laquila, Italy
来源
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS | 2002年 / 1569卷 / 1-3期
关键词
glutathione transferase; amphibia; mass spectrometry; N-terminal sequence; Xenopus laevis;
D O I
10.1016/S0304-4165(01)00238-0
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The expression of glutathione transferase isoenzymes has been investigated in embryo and adult liver of the frog Xenopus laevis. By analysing the GST isoenzymes recovered from GSH-affinity chromatography in terms of electrophoretic mobility, HPLC elution profile, immunological reactivity, N-terminal amino acid sequence and mass spectrometry molecular mass no significant difference in the GST subunit composition between embryos and liver was found. In both tissues the same three subunits, showing similarity to mu, alpha and sigma class GSTs, are present. These results, together with those previously reported for toad (Bufo bufo), strongly support the notion that the transition from an aquatic environment to a terrestrial atmosphere containing high oxygen concentration has accompanied specific GST gene expression. (C) 2002 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:81 / 85
页数:5
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