CLONING AND SEQUENCE-ANALYSIS OF CDNA FOR THE CA-2+-ACTIVATED PHOTOPROTEIN, CLYTIN

被引：61

作者：

INOUYE, S ^{[1
]}

TSUJI, FI ^{[1
]}

机构：

[1] UNIV CALIF SAN DIEGO, SCRIPPS INST OCEANOG, MARINE BIOL RES DIV 0202, LA JOLLA, CA 92093 USA

来源：

FEBS LETTERS | 1993年 / 315卷 / 03期

关键词：

BIOLUMINESCENCE; CA-2+-BINDING PROTEIN; COELENTERAZINE; CALCIUM; PHIALIDIN; AEQUORIN;

D O I：

10.1016/0014-5793(93)81191-2

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：

Clytin is a member of the aequorin family of photoproteins. It is made up of 189 amino acid residues, contains 3 Ca2+-binding sites, and shows 62% homology in amino acid residues to those in aequorin. The cysteine, tryptophan, and histidine residues, and the C-terminal proline, that are conserved in aequorin and clytin may be involved in the Ca2+-activated bioluminescence of the two proteins. Clytin may also prove useful in the determination of Ca2+.

引用

页码：343 / 346

页数：4

共 29 条

[1] EXTRACTION, PARTIAL-PURIFICATION AND PROPERTIES OF OBELIN, CALCIUM-ACTIVATED LUMINESCENT PROTEIN FROM HYDROID OBELIA-GENICULATA [J].