AMINO-ACID-SEQUENCE AND MOLECULAR CHARACTERIZATION OF A D-GALACTOSIDE-SPECIFIC LECTIN PURIFIED FROM SEA-URCHIN (ANTHOCIDARIS-CRASSISPINA) EGGS

被引：112

作者：

OZEKI, Y ^{[1
]}

MATSUI, T ^{[1
]}

SUZUKI, M ^{[1
]}

TITANI, K ^{[1
]}

机构：

[1] FUJITA HLTH UNIV, SCH MED, INST COMPREHENS MED SCI, DIV BIOMED POLYMER SCI, TOYOAKE, AICHI 47011, JAPAN

来源：

BIOCHEMISTRY | 1991年 / 30卷 / 09期

关键词：

D O I：

10.1021/bi00223a014

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 complete amino acid sequence of a 11.5-kDa subunit of D-galactoside binding lectin purified from sea urchin (Anthocidaris crassispina) eggs is presented. The 105-residue sequence of the subunit was determined by analysis of the intact S-carbamoylmethylated protein and peptides generated by digestion with Achromobacter protease I or Staphylococcus aureus V8 protease. The lectin exists as a disulfide-linked homodimer of two subunits; the dimeric form is essential for hemagglutination activity. However, the monomeric form obtained by partial reduction retains the carbohydrate binding capacity. Neither Ca2+ nor SH reagent is essential for hemagglutination or carbohydrate binding. The sequence has no similarity to that of any known protein and apparently represents a new type of galactoside binding lectin.

引用

页码：2391 / 2394

页数：4

共 24 条

[1] ECHINONECTIN - A NEW EMBRYONIC SUBSTRATE ADHESION PROTEIN [J].