Journal Article

Isolation, Properties and a Possible Function of a Water-Soluble Chlorophyll <i>a</i>/<i>b</i>-Protein from Brussels Sprouts

Yasumaro Kamimura, Takahiro Mori, Takenobu Yamasaki and Sakae Katoh

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 38, issue 2, pages 133-138
Published in print January 1997 | ISSN: 0032-0781
Published online January 1997 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/oxfordjournals.pcp.a029143
Isolation, Properties and a Possible Function of a Water-Soluble Chlorophyll a/b-Protein from Brussels Sprouts

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A water-soluble Chl a/b-protein (CP673) was isolated and purified from Brussels 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 there 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.

Keywords: Brassica oleracea L. var. gemmifera DC (Brussels sprouts); Chlorophyll a form; Drought-induced protein; Künitz type protease inhibitor; Water-soluble chlorophyll-protein

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Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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