PARTIAL-PURIFICATION AND CHARACTERIZATION OF DOPA QUINONE IMINE CONVERSION FACTOR FROM LARVAL HEMOLYMPH OF THE SILKWORM, BOMBYX-MORI

被引：5

作者：

ASO, Y

YAMAMOTO, K

YOSHINAGA, T

YAMAMOTO, H

YAMAGAMI, T

机构：

[1] Laboratory of Protein Chemistry and Engineering, Graduate School of Genetic Resources Technology, Kyushu University

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 1995年 / 59卷 / 02期

关键词：

D O I：

10.1271/bbb.59.277

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

DOPA quinone imine conversion factor was partially purified from larval hemolymph of the silkworm, Bombyx mori, using a novel assay. The factor was labile at 4 degrees C below pH 5 and above pH 11, and at pH 8.5 above 55 degrees C. Activity of the factor was maximal at pH 7.5-9, The factor catalyzed the decolorizations of L-DOPA methyl ester and alpha-methyl DOPA methyl ester chromes besides DOPA quinone imine. HPLC analysis indicated that the factor-catalyzed decolorization reaction of DOPA quinone imine resulted in the accumulation of dihydroxyindole, Based on spectral changes of alpha-methyl DOPA methyl ester chrome, it was suggested that the factor catalyzed the intramolecular oxidoreduction of DOPA quinone imine. During the oxidation of L-DOPA with endogenous phenoloxidase, the factor facilitated the formation of melanochrome.

引用

页码：277 / 281

页数：5

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