Open AccessThe closely related homomeric and heterodimeric mannose‐binding lectins from garlic are encoded by one‐domain and two‐domain lectin genes, respectively
Author(s) -
DAMME Els J. M.,
SMEETS Koen,
TORREKENS Sophie,
LEUVEN Fred,
GOLDSTEIN Irwin J.,
PEUMANS Willy J.
Publication year - 1992
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1992.tb16941.x
Subject(s) - lectin , complementary dna , allium sativum , homomeric , cd69 , biochemistry , biology , c type lectin , amino acid , mannan binding lectin , gene , ficolin , microbiology and biotechnology , nucleic acid sequence , peptide sequence , protein subunit , botany , cytotoxic t cell , il 2 receptor , in vitro
Lectin cDNA clones for two different lectins from garlic ( Allium sativum L.) bulbs, ASAI and ASAII (ASA, Allium sativum agglutinin), were isolated and characterized. the first lectin, ASAI, is a heterodimer composed of two different subunits of 11.5 kDa and 12.5 kDa. It is translated from an mRNA of 1400 nucleotides encoding a polypeptide of 306 amino acids with two very similar domains. N‐terminal sequenceing of the two polypeptides of the mature lectin confirmed that both subunits are derived from the same precursor and that each corresponds to one of the two domains in the sequence. In contrast to ASAI, the second garlic lectin, ASAII, is a homodimer of two identical 12‐kDa subunits. It is translated from an mRNA of approximately 800 nucleotides encoding a polypeptide of 154 amino acids. Interestingly, the coding region of the ASII cDNA clones is almost identical to that of the second domain of the ASAI cDNA clones.