COMPARISON OF N-TERMINAL AMINO-ACID-SEQUENCE OF FISH ROE RHAMNOSE-BINDING LECTINS

被引：16

作者：

HOSONO, M

MATSUDA, K

KAWAUCHI, H

TAKAYANAGI, Y

SHIOKAWA, H

MINEKI, R

MURAYAMA, K

NITTA, K

机构：

[1] TOHOKU COLL PHARMACEUT SCI,CANC RES INST,AOBA KU,SENDAI 981,JAPAN

[2] JUNTENDO UNIV,SCH MED,CENT LAB MED SCI,DIV BIOCHEM ANAL,BUNKYO KU,TOKYO 113,JAPAN

来源：

BIOMEDICAL RESEARCH-TOKYO | 1992年 / 13卷 / 06期

关键词：

D O I：

10.2220/biomedres.13.443

中图分类号：

R-3 [医学研究方法]; R3 [基础医学];

学科分类号：

1001 ;

摘要：

A 26-KDa rhamnose-binding lectin was purified from roe of shishamo smelt (Osmerus lanceolatus) by sequential chromatographies of DE23 anion exchange, D-galactose-Sepharose and TSK gel CM-5PW. This lectin (OLL) agglutinated rabbit and human ABO-type erythrocytes and sarcoma 180 cells. The lectin-induced hemagglutination was inhibited by L-rhamnose. The amino acid composition of OLL was similar to that of Osmerus eperlanus mordax roe lectin-4 (OML-4). The N-terminal 34 amino acid sequence of OLL was VTTDIXEGQQATLNXGSSVINVVSANYGRTDRVT (X: not defined) and similar to that of OML-4. Therefore, OLL and OML-4 may be the same lectin existing in the different species of fish roe.

引用

页码：443 / 449

页数：7

共 24 条

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