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IDENTIFICATION OF COVALENTLY BOUND FLAVIN OF L-GULONO-GAMMA-LACTONE OXIDASE

被引：51
作者：
KENNEY, WC
EDMONDSON, DE
SINGER, TP
NAKAGAWA, H
ASANO, A
SATO, R
机构：
[1] UNIV CALIF SAN FRANCISCO, DEPT BIOCHEM & BIOPHYS, SAN FRANCISCO, CA 94143 USA
[2] VET ADM HOSP, DIV MOLEC BIOL, SAN FRANCISCO, CA 94121 USA
[3] OSAKA UNIV, INST PROT RES, SUITA, OSAKA, JAPAN
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1976年 / 71卷 / 04期
关键词：
D O I：
10.1016/0006-291X(76)90780-4
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：
L-gulono-.gamma.-lactone oxidase contains a flavin moiety covalently linked to the protein. Properties of a partially purified flavin peptide, liberated by pronase digestion, indicate the presence of histidyl flavin, but not 8.alpha.-[N(3)-histidyl]-riboflavin. In the present study a purified tryptic-chymotryptic flavin peptide was acid-hydrolyzed to the amino acyl flavin (a mixture of its riboflavin level and its 2'',5''-anhydro form). High voltage electrophoresis, fluorescence excitation spectrum, and pKa of fluorescence quenching, in comparison with synthetic compounds, all show that 8.alpha.-[N(1)-histidyl]-riboflavin is the structure of the covalently bound flavin of this enzyme.
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页码：1194 / 1200
页数：7
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