Document Detail

Regulation of ribulose-1,5-bisphosphate carboxylase activity by the activase system in lysed spinach chloroplasts.
MedLine Citation:
PMID:  16666184     Owner:  NLM     Status:  PubMed-not-MEDLINE    
Ribulose-1,5-bisphosphate (RuBP) carboxylase in lysed spinach (Spinacia oleracea L. cv virtuosa) chloroplasts that had been partly inactivated at low CO(2) and Mg(2+) by incubating in darkness with 4 millimolar partially purified RuBP was reactivated by light. If purified RuBP was used to inhibit dark activation of the enzyme, reactivation by light was not observed unless fructose-1,6-bisphosphate, ATP, or ADP plus inorganic phosphate were also added. Presumably, ADP plus inorganic phosphate acted as an ATP-generating system with a requirement for the generation of DeltapH across the thylakoid membrane. When the RuBP obtained from Sigma Chemical Co. was used, light did not reactivate the enzyme. There was no direct correlation between DeltapH and activation. Therefore, thylakoids are required in the ribulose-1,5-bisphosphate carboxylase activase system largely to synthesize ATP. Inactivation of RuBP carboxylase in isolated chloroplasts or in the lysed chloroplast system was not promoted simply by a transition from light to dark conditions but was caused by low CO(2) and Mg(2+).
M A Parry; A J Keys; C H Foyer; R T Furbank; D A Walker
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Plant physiology     Volume:  87     ISSN:  0032-0889     ISO Abbreviation:  Plant Physiol.     Publication Date:  1988 Jul 
Date Detail:
Created Date:  2010-06-29     Completed Date:  2010-06-29     Revised Date:  2010-09-14    
Medline Journal Info:
Nlm Unique ID:  0401224     Medline TA:  Plant Physiol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  558-61     Citation Subset:  -    
AFRC Institute of Arable Crops Research, Rothamsted Experimental Station, Harpenden, Hertfordshire, United Kingdom, AL5 2JQ.
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