Isolation, properties and a possible function of a water-soluble chlorophyll a/b-protein from brussels sprouts [Brassica oleracea gemmifera]

• Published in: Plant and cell physiology 1997-02, Vol.38 (2), p.133-138
• Main Authors: Kamimura, Y. (Toho Univ., Funabashi, Chiba (Japan). Faculty of Science), Mori, T, Yamasaki, T, Katoh, S
• Format: Article
• Language: English
• Subjects: AGUA; Amino Acid Sequence; ANALYTICAL METHODS; Biological and medical sciences; BRASSICA OLERACEA GEMMIFERA; Brassica oleracea L. var. gemmifera DC (Brussels sprouts); Cell biochemistry; Cell physiology; Cell structures and functions; CHEMICOPHYSICAL PROPERTIES; Chlorophyll - genetics; Chlorophyll - isolation & purification; Chlorophyll - metabolism; Chlorophyll A; Chlorophyll a form; CHLOROPHYLLE; CHLOROPHYLLS; Chloroplast, photosynthetic membrane and photosynthesis; CLOROFILAS; Drought-induced protein; EAU; Fundamental and applied biological sciences. Psychology; Künitz type protease inhibitor; Light-Harvesting Protein Complexes; Molecular and cellular biology; Molecular Sequence Data; Photosynthetic Reaction Center Complex Proteins - genetics; Photosynthetic Reaction Center Complex Proteins - isolation & purification; Photosynthetic Reaction Center Complex Proteins - metabolism; Plant physiology and development; Plant Proteins - genetics; Plant Proteins - isolation & purification; Plant Proteins - metabolism; PROPIEDADES FISICOQUIMICAS; PROPRIETE PHYSICOCHIMIQUE; Protease Inhibitors - isolation & purification; Protease Inhibitors - metabolism; PROTEINAS; PROTEINE; PROTEINS; Sequence Homology, Amino Acid; SOLUBILIDAD; SOLUBILITE; SOLUBILITY; TECHNIQUE ANALYTIQUE; TECNICAS ANALITICAS; Vegetables - genetics; Vegetables - metabolism; WATER; Water-soluble chlorophyll-protein
• ISSN: 0032-0781; 1471-9053
• DOI: 10.1093/oxfordjournals.pcp.a029143

A water-soluble Chl a/b-protein (CP673) was isolated and purified from Burssels sprouts (Brassica oleracea L. var. gemmifera DC). The protein had a molecular mass of 78 kDa and an isoelectric point of 4.7, consisted of three or four subunits of 22 kDa and was extremely heat-stable. Although CP673 contained about one Chl a per protein, the blue and red absorption bands of Chl a that consisted of three or four Chl a forms with different absorption maxima suggested that these are several different modes or sites of binding for Chl a, Chl a/b ratio of larger than 10 also indicated that Chl b is present only in a small fraction of CP673. The heterogeneity of CP673 in terms of composition and binding of Chl suggests that Chl is not an intrinsic component of the Chl-protein. Homology search showed that the N-terminal amino acid sequence of CP673 is highly homologous with that of a 22 kDa protein that accumulates in water-stressed leaves of two Brassicaceae plants, rapeseed and radish, but not with those of the light-harvesting chl a/b-proteins of photosynthesis. A possible function of the water-soluble Chl-protein was discussed