Water-soluble chlorophyll protein of Brassica oleracea var. Botrys (cauliflower).
Water-soluble chlorophyll protein of Brassica oleracea var. Botrys (cauliflower).
复制标题
甘蓝的水溶性叶绿素蛋白。
DOI:
10.1016/0005-2728(71)90023-5
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发表时间:
1971
期刊:
影响因子:
--
通讯作者:
E. Yakushiji
中科院分区:
文献类型:
--
作者:
T. Murata;F. Toda;K. Uchino;E. Yakushiji
A water-soluble chlorophyll protein was prepared fromBrassica oleraceavar. Botrys (cauliflower) and purified by (NH4)2SO4fractionation and by chromatography on a DEAE-cellulose column. The chlorophyll protein contained chlorophyllsaandbin the ratio 6:1, and no carotenoids. The molecular weight, determined by means of gel filtration on Sephadex G-100, was 78000. The chlorophyll protein showed absorption peaks at 273, 340, 384, 420, 438, 465, 628, 674 and 700 nm. Since the three bands at 384, 420 and 438 nm all have approximately the same height, the spectrum is different from that of chlorophyllain organic solvents. The fluorescence of the chlorophyll protein showed a peak at 683 nm, with shoulders at 706 and 745 nm at room temperature, and peaks at 685, 706 and 744 nm at the temperature of liquid N2. An apo-protein was prepared by removing the chlorophylls with 2-butanone and purified by precipitation with (NH4)2SO4. The apo-protein thus prepared had an absorption band at 273 nm but none at longer wavelengths. The apo-protein could be combined with chlorophylls, forming a chlorophyll protein which had spectral characteristics similar to those of the original.