Cloning and sequence analysis of the Maackia amurensis haemagglutinin cDNA.

Abstract:

:Maackia amurensis haemagglutinin (MAH) is a leguminous lectin which preferentially binds to a cluster of sialylated O-linked carbohydrate chains (Konami Y, Yamamoto K. Osawa T, Irimura T (1994) FEBS Lett 342:334-38). In the present study a 950 bp cDNA clone encoding MAH was isolated from a cDNA library constructed from germinated Maackia amurensis seeds. From the nucleotide sequence, MAH was predicted to consist of 285 amino acid residues containing a signal peptide of 29 amino acids. The results also confirmed our previous findings from the amino acid sequence analysis, which indicated that two highly conserved amino acid residues in all other well-known leguminous lectins were replaced in MAH. These residues were lysine-105 and aspartic acid-135. The corresponding amino acid residues in other leguminous lectins were glycine and asparagine, respectively. These differences were due to the presence of nucleotides AAA and GAT in place of AAT/C and GGA/T.

journal_name

Glycoconj J

journal_title

Glycoconjugate journal

authors

Yamamoto K,Ishida C,Saito M,Konami Y,Osawa T,Irimura T

doi

10.1007/BF00731308

subject

Has Abstract

pub_date

1994-12-01 00:00:00

pages

572-5

issue

6

eissn

0282-0080

issn

1573-4986

journal_volume

11

pub_type

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