Ribulose bisphosphate carboxylase of high specific activity from anther-derived haploid plants of Nicotiana tabacum

Conference · Tue Apr 01 00:00:00 EST 1986 · Plant Physiol., Suppl.; (United States)

OSTI ID:5332319

Bhaskaran, S; Burdick, P J; Smith, R H

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), Vol. 80:4; Conference: Annual meeting of the American Society of Plant Physiologists, Baton Rouge, LA, USA, 8-12 Jun 1986
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
CARBOXYLASE
LABELLING
PRODUCTION
NICOTIANA
ENZYME ACTIVITY
VEGETATIVE PROPAGATION
CARBON 14
CARBON 14 COMPOUNDS
ENZYMES
HAPLOIDY
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
CARBON ISOTOPES
CARBON-CARBON LYASES
CARBOXY-LYASES
CLONING
EVEN-EVEN NUCLEI
ISOTOPES
LABELLED COMPOUNDS
LIGHT NUCLEI
LYASES
NUCLEI
PLANTS
PLOIDY
RADIOISOTOPES
YEARS LIVING RADIOISOTOPES
550201* - Biochemistry- Tracer Techniques