Purification and cDNA cloning of a novel factor produced by a human T-cell hybridoma: sequence homology with animal lectins.
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Yoshimatsu K, Ohya Y, Shikata Y, Seto T, Hasegawa Y, Tanaka I, Kawamura T, Kitoh K, Toyoshima S, Osawa T
Purification and cDNA cloning of a novel factor produced by a human T-cell hybridoma: sequence homology with animal lectins.
Mol Immunol. 1992 Apr;29(4):537-46.
- PubMed ID
- 1565101 [ View in PubMed]
- Abstract
We have purified a novel immunoregulatory factor (BMPG: bone-marrow proteoglycan) produced by a T-cell hybridoma, with a monoclonal antibody column. Using an oligonucleotide probe corresponding to the partial amino acid sequence of BMPG, we cloned, sequenced, and expressed a cDNA for BMPG. BMPG has 222 amino acid residues with a 16 N-terminal signal sequence, so the mature form has 206 amino acid residues. BMPG was found to have unique characteristics: it has three types of sugar chains and it shows a marked homology with animal lectins including the human asialoglycoprotein receptor, chicken hepatic lectin and the homing receptor of lymphocytes.