Water-soluble chlorophyll protein of Brassica oleracea var. Botrys (cauliflower).

Water-soluble chlorophyll protein of Brassica oleracea var. Botrys (cauliflower).
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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:
Biochimica et biophysica acta
影响因子:
--
通讯作者:
E. Yakushiji
E. Yakushiji
中科院分区:
--
文献类型:
--
作者:
T. Murata;F. Toda;K. Uchino;E. Yakushiji

文献摘要

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以甘蓝为原料制备了一种水溶性叶绿素蛋白。通过(NH 4)2SO 4分级分离和在DEAE-纤维素柱上层析来纯化。叶绿素蛋白中叶绿素与叶绿素的比例为6:1,不含类胡萝卜素.用Sephadex G-100凝胶过滤法测定其分子量为78000。叶绿素蛋白在273、340、384、420、438、465、628、674和700 nm处有吸收峰。由于在384、420和438 nm处的三个谱带都具有大致相同的高度,因此光谱不同于叶绿素有机溶剂的光谱。在室温下,叶绿素蛋白的荧光峰位于683 nm,肩峰位于706和745 nm,在液氮温度下,荧光峰位于685、706和744 nm。用2-丁酮去除叶绿素制备脱辅基蛋白,并用(NH 4)2SO 4沉淀纯化。如此制备的脱辅基蛋白在273 nm处具有吸收带,但在更长的波长处没有吸收带。脱辅基蛋白可以与叶绿素结合,形成具有与原始蛋白相似光谱特性的叶绿素蛋白。
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.