Pawar, AshwiniGoswami - Giri, Anita2012-03-312012-03-312012-030974-4169http://dspace.vpmthane.org:8080/jspui/handle/123456789/2541Separation of Ribulose-1, 5-bisphosphate carboxylase/oxygenase (Rubisco) with its naturally tightly bound inhibitor 2- Carboxyarabinitol-1-phosphate (Ca-1P) from leaves of Solanum xanthocarpum was carried out using polyethylene glycol precipitation method. The inhibitor was purified by ion exchange chromatography. The potential of Rubisco activity was determined by the relative rate of biosynthesis and degradation. Rubisco had a Mass of 55 KDa with two subunits, LSU (55 KD) and SSU (14 KD) showing single peak on HPLC. Properties of isolated CA1-P were analyzed by TLC, HPLC, UV, IR and LC-MS. Rubisco efficiency may potentially lead to a faster plant growth, quicker sequestration of CO2 from the air and more efficient of plant removal of green house gases from the atmosphere.enPhotosynthesisRubiscoCa-1P, Solanum xanthocarpum Lenzyme regulationenzyme inhibitorArticle