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., Bagi, F., Mesterházy, Aring;., Szécsi, Á.: Isozyme evidence of two groups of Fusarium graminearum. Mycol Res 104 , 788-793 (2000). Isozyme evidence of two groups of Fusarium graminearum Mycol Res

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Buso, G., Rangel, P. and Ferreira, M. (1998): Analysis of genetic variability of South American wild rice populations (Oryza glumaepatula) with isozymes and RAPD markers. — Mol. Ecol. 7 : 107

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binding domain of rat steroid 5α-reductase (isozyme-1): the steroid D-ring binding domain of 5α-reductase. Steroids 64 , 197–204. Collins D. C. Analysis of the steroid binding

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927 Láday, M., Bagi, F., Mesterházy, Á. and Szécsi, Á. (2000): Isozyme evidence for two groups of Fusarium graminearum. Mycol. Res. 104, 788-793. Isozyme evidence

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Francisco. Numerical taxonomy Vágvölgyi, Cs., Papp, T., Palágyi, Zs., Michailides, T. J. (1996) Isozyme variation among isolates of Mucor

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Fructose-bisphosphate aldolase (FBA, EC 4.1.2.13) catalyzes an aldol cleavage of fructose-1, 6-bisphosphate to dihydroxyacetone-phosphate and glyceraldehyde 3-phosphate and a reversible aldol condensation. Three candidate genes with 1077bp coding for fructose-bisphosphate aldolase were cloned and sequenced in wheat, barley and rye. These genes could encode 358 amino acid residues. Sequence analysis indicated that wheat, barley and rye FBA genes were conserved with high identity (94.13%), while maize sequence had a 9bp deletion near the 3’ terminal. According to the alignment of 75 amino acid sequences, conserved domains of the FBAs were detected. These conserved domains might be the important functional sites of the FBAs. The cytoplasmic FBAs of wheat, barley and rye were clustered together, and the cluster was close to maize and rice FBAs. Nine peptides of the FBAs and the last amino acid Tyr (necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate) were most conserved in plants, animals and algae. Current findings suggested that the FBAs could be divided into three main subgroups: plant cytoplasmic FBA, plant chloroplastic FBA and animal FBA. These results also indicated that the active and binding sites of FBAs had rare variations during the long-term evolution.

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522 536 Woodbury, W., Spensen, A. K., Stahman, M. (1971): An improved procedure using ferricyanide for detecting catalase isozymes. Anal. Biochem. , 44 , 301

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Cohen, E. (1976): Esterase isozymes of some Tribolium strains. Tribolium Inf. Bull. 19 : 120-125. Esterase isozymes of some Tribolium strains Tribolium Inf. Bull

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