A1 Refereed original research article in a scientific journal
RUBISCO SUBUNIT BINDING-PROTEIN INCREASES THE SOLUBILITY OF RUBISCO LARGE SUBUNIT INVITRO
Authors: RINTAMAKI E
Publisher: ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
Publication year: 1991
Journal: Plant Physiology and Biochemistry
Journal name in source: PLANT PHYSIOLOGY AND BIOCHEMISTRY
Journal acronym: PLANT PHYSIOL BIOCH
Volume: 29
Issue: 1
First page : 1
Last page: 8
Number of pages: 8
ISSN: 0981-9428
Abstract
The effect of Rubisco (ribulose-1,5-bisphosphate carboxylase-oxygenase, EC 4.1.1.39) subunit binding protein (BP) on the solubility of Rubisco large subunits was studied in an in vitro experiment, using Rubisco and BP preparations purified from wheat seedlings (Triticum aestivum). The Rubisco molecule was dissociated into subunits at pH 5 in the absence and presence of BP. In the absence of BP the large subunits aggregated, and did not redissolve in neutral buffer without the addition of detergent and mercaptoethanol. Where BP was present during the dissociation of the Rubisco, large subunits associated with the BP complex, and showed increased solubility in neutral buffer. The result suggests that specific binding of large subunits to the BP complex reduces the tendency of these polypeptides to associate incorrectly with one another.
The effect of Rubisco (ribulose-1,5-bisphosphate carboxylase-oxygenase, EC 4.1.1.39) subunit binding protein (BP) on the solubility of Rubisco large subunits was studied in an in vitro experiment, using Rubisco and BP preparations purified from wheat seedlings (Triticum aestivum). The Rubisco molecule was dissociated into subunits at pH 5 in the absence and presence of BP. In the absence of BP the large subunits aggregated, and did not redissolve in neutral buffer without the addition of detergent and mercaptoethanol. Where BP was present during the dissociation of the Rubisco, large subunits associated with the BP complex, and showed increased solubility in neutral buffer. The result suggests that specific binding of large subunits to the BP complex reduces the tendency of these polypeptides to associate incorrectly with one another.
UTU Research Portal