A new form of crystalline rubisco and the conversion to its common dodecahedral form.
In this paper, we present a new purification procedure that yields a new crystalline form of rubisco and has enabled us to completely remove this most abundant protein from tobacco leaf extract. The crystals formed within 48 h after refrigeration at 4 degrees C at pH 5.6. However, these crystals were not well-ordered crystals and lacked well-defined facets or edges. The remaining leaf extract (fraction 2 protein) was void of rubisco. Conversion of this new crystalline form of rubisco to its common dodecahedral form was achieved by dialysing the protein solution in Tris buffer at pH 8.0 or purified water. Since the molecular size of its large subunit of rubisco (55 kD) is similar to that of the papillomavirus capsid protein, L1 (57 kD), its complete removal from fraction 2-protein may facilitate the detection, purification, and recovery of the Li protein.
Kwanyuen
Prachuab
P
United States Department of Agriculture, Agricultural Research Service and Crop Science Department, North Carolina State University, Raleigh, North Carolina 27695-7631, USA. prachuab_kwanyuen@ncsu.edu
Allina
Sandra M
SM
Weissinger
Arthur K
AK
Wilson
Richard F
RF
D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D011487:Protein Conformation; D012273:Ribulose-Bisphosphate Carboxylase / Q000737:chemistry* / Q000302:isolation & purification*; D013696:Temperature; D013997:Time Factors; D014026:Nicotiana / Q000378:metabolism
D012273:Ribulose-Bisphosphate Carboxylase