Morphological, cytological, isozyme and chloroplast DNA analyses were used to determine possible mechanism(s) for the loss of glutamate oxaloacetate transaminase-4 (GOT-4) isozyme activity in a somatic hybrid. Plant 204-1, derived by cell fusion between tomato (Lycopersicon esculentum) and Solanum l
Glutamate oxaloacetate transaminase isozymes of theTriticinae: dissociation and recombination of subunits
โ Scribed by G. E. Hart; P. J. Langston
- Publisher
- Springer
- Year
- 1977
- Tongue
- English
- Weight
- 590 KB
- Volume
- 50
- Category
- Article
- ISSN
- 0040-5752
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โฆ Synopsis
A simple procedure has been developed for the dissociation of active molecules of glutamate oxaloacetate transaminase (GOT: E.C. 2.6.1.1) into protomers and for the reassociation of the subunits into active enzymes. Results of experiments in which the protomers of genetically controlled electrophoretic variants of GOT of Triticum aestivum and of several related species were dissociated and recombined in crude tissue extracts and in partially purified preparations support the hypothesis that the enzyme exists functionally as a dimer in the Triticinae.
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The multiple forms of glutamate oxaloacetate transaminase in the annual diploid plant Stephanomeria exigua (Compositae) are controlled by three unlinked gene loci with two, four, and five alleles, respectively. All alleles are codominant, and heterozygotes for any pair of them produce a more darkly
Glutamate oxaloacetic transaminase (L-aspertate: 2-oxoglutarate aminotransferase, E.C. 2.6.1.1; GOT) was found to occur in five distinct electrophoretic forms in different tissue extracts from a number of highly inbred strains of Zea mays L. No major qualitative differences were detected in the vari