| Literature DB >> 1565101 |
K Yoshimatsu1, Y Ohya, Y Shikata, T Seto, Y Hasegawa, I Tanaka, T Kawamura, K Kitoh, S Toyoshima, T Osawa.
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.Entities:
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Year: 1992 PMID: 1565101 DOI: 10.1016/0161-5890(92)90012-m
Source DB: PubMed Journal: Mol Immunol ISSN: 0161-5890 Impact factor: 4.407