Isolation and complete amino-acid sequence of the small polypeptide from light-harvesting pigment-protein complex I (B870) of Rhodopseudomonas capsulata.
The small bacteriochlorophyll-binding polypeptide of the light-harvesting complex B870 was extracted from the intracytoplasmic membrane of the strain A1a+ of Rhodopseudomonas capsulata with chloroform/methanol/ammonium acetate and separated by chromatography on Sephadex LH60 using the same solvent. The polypeptide obtained from the peak fraction III was found to be homogeneous and identical with the small polypeptide isolated from the B870 complex as shown by dodecyl sulfate/polyacrylamide gel electrophoresis, amino acid composition and N-terminal sequence. The complete amino acid sequence is given. The relative molecular mass based on the amino acid sequence is 5341. The polarity of amino acids is 35.42%. The C-terminal part of the peptide chain from residue 29 to 48 is hydrophobic and includes one His residue.
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000302:isolation & purification*; D002268:Carboxypeptidases; D003488:Cyanogen Bromide; D045342:Light-Harvesting Protein Complexes; D010446:Peptide Fragments / Q000302:isolation & purification*; D045322:Photosynthetic Reaction Center Complex Proteins; D012241:Rhodopseudomonas / Q000032:analysis*
D001426:Bacterial Proteins; D045342:Light-Harvesting Protein Complexes; D010446:Peptide Fragments; D045322:Photosynthetic Reaction Center Complex Proteins; D002268:Carboxypeptidases; D003488:Cyanogen Bromide