Rubisco was extracted and purified from leaves of nineteen Avena spe-cies. The holoenzyme shows the already known “slow” and “fast” forms after native electrophoresis. The electrophoresis in denaturing conditions revealed a unique poly-peptide for the large subunit and two types of polypeptides for the small subunit. The addition of leupeptin, a thiol proteinase Inhibitor, during purification of the holoenzyme, reduced microheterogeneity within both subunit types. Subunit composition of the enzyme appears to be a taxonomic tool for distinguishing three species: A. clauda Dur., A. eriantha Dur. and A. cattariensis Baum. Rajh. et Baum. © Taylor & Francis Group, LLC.
Conte L., Cristofolini G., Bonomo M.C. (1996). Subunits polypeptide composition of rubisco in avena species. GIORNALE BOTANICO ITALIANO, 130(2-3), 567-573 [10.1080/11263509609430325].
Subunits polypeptide composition of rubisco in avena species
Conte L.;Cristofolini G.;Bonomo M. C.
1996
Abstract
Rubisco was extracted and purified from leaves of nineteen Avena spe-cies. The holoenzyme shows the already known “slow” and “fast” forms after native electrophoresis. The electrophoresis in denaturing conditions revealed a unique poly-peptide for the large subunit and two types of polypeptides for the small subunit. The addition of leupeptin, a thiol proteinase Inhibitor, during purification of the holoenzyme, reduced microheterogeneity within both subunit types. Subunit composition of the enzyme appears to be a taxonomic tool for distinguishing three species: A. clauda Dur., A. eriantha Dur. and A. cattariensis Baum. Rajh. et Baum. © Taylor & Francis Group, LLC.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
