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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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Sevinc A, Sari R, Fadillioglu E, Gaziantep AM: The utility of lactate dehydrogenase isozyme pattern in the diagnostic evaluation of malignant and non malignant ascites. J. Natl. Med. Assoc. 97(1), 79–84 (2005

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

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Phytophthora alni is a species hybrid that causes a destructive root and collar rot disease of alders throughout Europe. Its subspecies, P. alni subsp. alni (Paa), P. alni subsp. uniformis (Pau) and P. alni subsp. multiformis (Pam) can be distinguished on the basis of phenotypic and genotypic traits. In this study, we report evidence of an unusual genomic combination of two subspecies occurring in two P. alni isolates from Hungary. These isolates, which had previously been identified as Paa using hybrid-specific PCR primers and morphological traits, exhibited a mitochondrial DNA restriction pattern identical to that of Pau. However, RAPD patterns and isozyme profiles of nuclear genes encoding glucose-phosphate isomerase (Gpi) and malate dehydrogenase (Mdh) of the two atypical isolates were identical to those found in all Paa isolates. Isozyme analysis also revealed a novel allele at the putative Mdh-1 locus in Paa and Pam isolates. The atypical Paa isolates have likely emerged as a result of hybridization events in the P. alni population between Paa and Pau .

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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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