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Publication Type:
| Report |
Content Type: | Abstract or Summary only |
Author(s): | Scott, J. S.;
Bruno, P.;
David, N. R.;
Rapp, B. J.;
Randall, D. D. |
Author Affiliation: | Biochemistry Department, University of Missouri |
Title: | RuBP carboxylase: Crystallization and subunit composition of enzyme from polyploid Festuca arundinacea |
Source: | Plant Physiology. Vol. 27, No. 1, May 1983, p. . |
Publishing Information: | Lancaster, PA: American Society of Plant Physiologists |
Keywords: | TIC Keywords: Festuca arundinacea; Carboxylase; Enzymes; Enzyme activators; Enzyme inhibitors
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Abstract/Contents: | "RuBP carboxylase was purified from polyploid genotypes of tall fescue, Festuca arundinacea in the presence of activators and protease inhibitors. The purified carboxylase exhibits doublet large subunit (LSU) and doublet small subunit (SSU) on dissociating gradient PAGE, one protein band on native PAGE and 4 to 8 polypeptides on dissociating isoelectric focusing gels. The percentage of total protein in one of these IEF polypeptides correlated with the net photosynthesis rates in the polyploid genotypes. RuBP carboxylase was crystalized from ployethlene glycol colutions. The enzyme crystals were similar from 2 genotypes which show a 2-fold difference in net photosynthesis and RuBP carboxylase levels. The different subunits and polypeptides patterns may help indicate the genomic background of the alloploidy fescues under study." |
Language: | English |
References: | 0 |
Note: | This item is an abstract only! |
| ASA/CSSA/SSSA Citation (Crop Science-Like - may be incomplete): Scott, J. S., P. Bruno, N. R. David, B. J. Rapp, and D. D. Randall. 1983. RuBP carboxylase: Crystallization and subunit composition of enzyme from polyploid Festuca arundinacea. Plant Physiol. 27(1) |
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