CLONING, EXPRESSION AND SEQUENCE-ANALYSIS OF CDNA FOR THE CA2+-BINDING PHOTOPROTEIN, MITROCOMIN

被引：56

作者：

FAGAN, TF

OHMIYA, Y

BLINKS, JR

INOUYE, S

TSUJI, FI

机构：

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

[2] OSAKA BIOSCI INST, SUITA, OSAKA 565, JAPAN

[3] UNIV WASHINGTON, FRIDAY HARBOR LABS, FRIDAY HARBOR, WA 98250 USA

来源：

FEBS LETTERS | 1993年 / 333卷 / 03期

关键词：

BIOLUMINESCENCE; HALISTAURA; CALCIUM; AEQUORIN; CLYTIN; C-TERMINAL TYROSINE;

D O I：

10.1016/0014-5793(93)80675-K

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：

The primary structure of mitrocomin consists of 190 amino acid residues, with three Ca2+-binding sites and a tyrosine residue at tbe C-terminus. Mitrocomin shows an amino acid sequence homology of 67.9% and 60.7% when compared with aequorin and clytin, respectively. The amino acid residues Cys152, His58, His169, Trp12, Trp86, Trp108, Trp129 and Trp173 are conserved in all three photoproteins, suggesting that they play a role in light emission.

引用

页码：301 / 305

页数：5

共 29 条

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