PMID- 24264746
OWN - NLM
STAT- PubMed-not-MEDLINE
DCOM- 20131126
LR  - 20211021
IS  - 0032-0935 (Print)
IS  - 0032-0935 (Linking)
VI  - 158
IP  - 4
DP  - 1983 Aug
TI  - Ribulose 1,5-bisphosphate carboxylase and phosphoribulokinase in Prochloron.
PG  - 281-7
LID - 10.1007/BF00397328 [doi]
AB  - Cell-free extracts of Prochloron didemni were assayed for ribulose 
      1,5-bisphosphate (RuBP) carboxylase (EC 4.1.1.39) and phosphoribulokinase (EC 
      2.7.1.19), two key enzymes in the reductive pentose-phosphate cycle. In an 
      RuBP-dependent reaction, the production of two molecules of 3-phosphoglycerate 
      per molecule of CO2 fixed was shown. Phosphoribulokinase activity was 
      demonstrated by the production of ADP from ribulose 5-phosphate (Ru5P) and ATP 
      and by measurement of ATP-, Ru5P-dependent (14)CO2 fixation in the presence of 
      excess spinach RuBP carboxylase. When Prochloron RuBP carboxylase was purified 
      from cell-free extracts by isopycnic centrifugation in reoriented linear 0.2 to 
      0.8 M sucrose gradients, the enzyme sedimented to a position which corresponded 
      to that for the 520,000-dalton spinach enzyme. After polyacrylamide gel 
      electrophoresis (PAGE) of Prochloron enzyme, a major band of enzyme activity 
      corresponded to that for the spinach enzyme. Considerably more additional 
      carboxylase activity was found in a less mobile species than was the case for 
      spinach RuBP carboxylase. Sodium dodecyl sulfate-PAGE of the Prochloron enzyme 
      indicates that it is composed of both large (molecular weight, MW=57,500) and 
      small (MW=18,800) subunits.
FAU - Berhow, M A
AU  - Berhow MA
AD  - Biochemistry/Biophysics Program, Washington State University, 99164-4660, 
      Pullman, WA, USA.
FAU - McFadden, B A
AU  - McFadden BA
LA  - eng
PT  - Journal Article
PL  - Germany
TA  - Planta
JT  - Planta
JID - 1250576
EDAT- 1983/08/01 00:00
MHDA- 1983/08/01 00:01
CRDT- 2013/11/23 06:00
PHST- 1982/10/28 00:00 [received]
PHST- 1983/03/21 00:00 [accepted]
PHST- 2013/11/23 06:00 [entrez]
PHST- 1983/08/01 00:00 [pubmed]
PHST- 1983/08/01 00:01 [medline]
AID - 10.1007/BF00397328 [doi]
PST - ppublish
SO  - Planta. 1983 Aug;158(4):281-7. doi: 10.1007/BF00397328.