Mitochondrial polymorphism. III. Heterosis, complementation, and spectral properties of purified cytochrome oxidase of wheat
✍ Scribed by Igor V. Sarkissian; Hari K. Srivastava
- Book ID
- 104784855
- Publisher
- Springer
- Year
- 1971
- Tongue
- English
- Weight
- 373 KB
- Volume
- 5
- Category
- Article
- ISSN
- 0006-2928
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✦ Synopsis
Cytochrome oxidase was purified twentyfold from mitochondria of seedlings of wheat genotypes 28, 31 MS, and 31 MS/28. The enzyme of the hybrid exceeded in activity the parental enzymes. Mixtures of cytochrome oxidase of the parents exhibited eomplementation in that they approached the activity of the hybrid cytoehrome oxidase. Hybrid mitochondria also exhibited heterosis in NADH: cytochrome c reductase activity. Complementation by parent mitochondria was observed for this enzyme also. The Michaelis constant of cytochrome oxidase and NADH : eytoehrome reduetase was markedly less in the hybrid and the mixture than in the parents. Difference spectra revealed the following: strain 28 had cytochromes a and b but was deficient in cytochrome c; strain 31 MS had cytoehromes b and c but no a; the hybrid had all three eytochromes, as did the mixture. The relationship of cytochromes to heterosis and eomplementation is considered.