Ribulose bisphosphate carboxylase of high specific activity from anther-derived haploid plants of Nicotiana tabacum
Crystalline ribulose bisphosphate carboxylase was purified from several haploid plants of Nicotiana tabacum obtained by anther-culture. Specific activity of the enzyme ranged from 1.09 to 2.15 ..mu..moles /sup 14/CO/sub 2/ fixed mg protein/sup -1/ min/sup -1/ in growth chamber grown plants and 0.5 to 1.15 ..mu..moles /sup 14/CO/sub 2/ fixed mg protein/sup -1/ min/sup -1/ in greenhouse grown plants. No degradation of the large subunit was observed on SDS-PAGE electrophoresis of these purified preparations. A low specific activity of 0.25 units was obtained for a preparation of the enzyme from a plant grown under fluctuating growth conditions. This protein gave an additional band for the large subunit on electrophoresis, presumably a degradation product. Individual differences in specific activity under identical growth conditions in these haploids suggest a possible role for the small subunit in regulation of enzyme activity.
- Research Organization:
- Texas A and M Univ., College Station
- OSTI ID:
- 5332319
- Journal Information:
- Plant Physiol., Suppl.; (United States), Journal Name: Plant Physiol., Suppl.; (United States) Vol. 80:4; ISSN PPYSA
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
59 BASIC BIOLOGICAL SCIENCES
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
CARBON 14
CARBON 14 COMPOUNDS
CARBON ISOTOPES
CARBON-CARBON LYASES
CARBOXY-LYASES
CARBOXYLASE
CLONING
ENZYME ACTIVITY
ENZYMES
EVEN-EVEN NUCLEI
HAPLOIDY
ISOTOPES
LABELLED COMPOUNDS
LABELLING
LIGHT NUCLEI
LYASES
NICOTIANA
NUCLEI
PLANTS
PLOIDY
PRODUCTION
RADIOISOTOPES
VEGETATIVE PROPAGATION
YEARS LIVING RADIOISOTOPES