Purification and characterization of multiple glutathione transferase isoenzymes from grey mullet liver
作者： E. Mart�nez-Lara , S. G. George , J. L�pez-Barea , J. A. B�rcena
关键词: Glutathione 、 Biochemistry 、 Mullet 、 Population 、 Gene isoform 、 Mugil 、 Molecular biology 、 Protein subunit 、 Molecular mass 、 Biology 、 Isozyme
摘要: Fourteen isoforms of glutathione S-transferase (GST) have been separated and purified from mullet (Mugil cephalus) liver by scaling up an automatic analytical method based on anionic exchange chromatography. The activity each isoenzyme with several substrates was determined. Dimeric combinations six subunits make this heterogeneous population. Five these were resolved reverse phase chromatography; four them, named a, b, c d, present in more than one isoform, had the same apparent molecular mass (25.2 kDa) SDS-PAGE, immunochemically related to plaice GST-A possibly rat GST-5 but not GST-B or any other GST subunit; they would belong theta class. Subunit e only I which basic, 23.4 kDa alpha class, since it recognized antibodies towards GST-1 GST-8 less intensely anti-(rat)GST-2. Another subunit, f, 25.2 that could be distin guished chromatography, detected positive reaction GST-2 addition anti-(plaice)GST-A. As suggested results we discuss existence genetic polymorphism, differential expression evolutionary relationships GSTs.
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sci-hub.se 参考文章(32)
Horng-I. YEH, Jing-Yu LEE, Shu-Ping TSAI, Cheng-Hsilin HSIEH, Ming F. TAM, Rat kidney glutathione S-transferase 1 subunits have C-terminal truncations. Biochemical Journal. ,vol. 314, pp. 1017- 1025 ,(1996) , 10.1042/BJ3141017
Carl R. Merril, David Goldman, Margaret L. Van Keuren, Gel protein stains: silver stain. Methods in Enzymology. ,vol. 104, pp. 441- 447 ,(1984) , 10.1016/S0076-6879(84)04111-2
William H. Habig, William B. Jakoby, [27] Glutathione S-transferases (rat and human) Methods in Enzymology. ,vol. 77, pp. 218- 231 ,(1981) , 10.1016/S0076-6879(81)77029-0
C P Tu, C C Reddy, On the multiplicity of rat liver glutathione S-transferases. Journal of Biological Chemistry. ,vol. 260, pp. 9961- 9964 ,(1985) , 10.1016/S0021-9258(17)39194-9
A K Ostlund Farrants, D J Meyer, B Coles, C Southan, A Aitken, P J Johnson, B Ketterer, The separation of glutathione transferase subunits by using reverse-phase high-pressure liquid chromatography Biochemical Journal. ,vol. 245, pp. 423- 428 ,(1987) , 10.1042/BJ2450423
T. Igarashi, A. Kohara, Y. Shikata, F. Sagami, J. Sonoda, T. Horie, T. Satoh, The unique feature of dog liver cytosolic glutathione S-transferases. An isozyme not retained on the affinity column has the highest activity toward 1,2-dichloro-4-nitrobenzene. Journal of Biological Chemistry. ,vol. 266, pp. 21709- 21717 ,(1991) , 10.1016/S0021-9258(18)54694-9
Leopold Flohé, Wolfgang A. Günzler, ASSAYS OF GLUTATHIONE PEROXIDASE Methods in Enzymology. ,vol. 105, pp. 114- 121 ,(1984) , 10.1016/S0076-6879(84)05015-1
P.I.N. Ramage, G.H. Rae, I.A. Nimmo, Purification and properties of the hepatic glutathione of the Atlantic Salmon (Salmo salar) Comparative Biochemistry and Physiology Part B: Comparative Biochemistry. ,vol. 83, pp. 23- 29 ,(1986) , 10.1016/0305-0491(86)90326-3
William H. Habig, Michael J. Pabst, William B. Jakoby, Glutathione S-Transferases Journal of Biological Chemistry. ,vol. 249, pp. 7130- 7139 ,(1974) , 10.1016/S0021-9258(19)42083-8
Yuichi Sugiyama, Tadataka Yamada, Neil Kaplowitz, Glutathione S-transferases in elasmobranch liver. Molecular heterogeneity, catalytic and binding properties, and purification Biochemical Journal. ,vol. 199, pp. 749- 756 ,(1981) , 10.1042/BJ1990749