Polypeptide Composition of Chlorophyll-Protein Complexes from Romaine Lettuce 1
AUTOR(ES)
Henriques, Fernando
RESUMO
The protein moiety of the two major chlorophyll-protein complexes associated with chloroplast membranes of outer, dark green leaves of a romaine lettuce shoot (Lactuca sativa L. var. Romana) has been analyzed by discontinuous sodium dodecyl sulfate-polyacrylamide disc gel electrophoresis. Complex II, also termed light-harvesting chlorophyll-protein complex, is shown to consist of a major polypeptide of 25 kilodaltons (kD) and two minor ones of 27.5 and 23 kD. The 25 kD subunit is the single largest polypeptide component of the chloroplast membranes, accounting for about 25% of their total protein. Complex I contains only high molecular weight subunits, the major one being at 67 kD, these subunits representing only a small percentage of the chloroplast membrane total protein.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=542549Documentos Relacionados
- Chlorophyll-Protein Complexes of the Cyanophyte, Nostoc sp. 1
- Fractionation of Thylakoid Membranes with the Nonionic Detergent Octyl-β-d-glucopyranoside: RESOLUTION OF CHLOROPHYLL-PROTEIN COMPLEX II INTO TWO CHLOROPHYLL-PROTEIN COMPLEXES
- Chlorophyll biosynthesis and assembly into chlorophyll-protein complexes in isolated developing chloroplasts
- Higher plant chloroplasts: Evidence that all the chlorophyll exists as chlorophyll—protein complexes
- Widespread Distribution of Some Minor Chlorophyll-Protein Complexes in Some Plants and Algae