Isolation and complete amino‐acid sequence of the small polypeptide from light‐harvesting pigment‐protein complex I (B870) of Rhodopseudomonas capsulata

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Abstract
The small bacteriochlorophyll-binding polypeptide of the light-harvesting complex B870 was extracted from the intracytoplasmic membrane of the strain Ala+ of R. 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 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 29-48 is hydrophobic and includes 1 His residue.