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Purification and cDNA cloning of a novel factor produced by a human T-cell hybridoma: Sequence homology with animal lectins
- Source :
- Molecular Immunology. 29:537-546
- Publication Year :
- 1992
- Publisher :
- Elsevier BV, 1992.
-
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.
- Subjects :
- Signal peptide
T-Lymphocytes
Molecular Sequence Data
Restriction Mapping
Immunology
Sequence alignment
Molecular cloning
Biology
Chromatography, Affinity
Eosinophil Major Basic Protein
Lectins
Sequence Homology, Nucleic Acid
Complementary DNA
Animals
Humans
Amino Acid Sequence
Cloning, Molecular
Molecular Biology
Peptide sequence
Hybridomas
Base Sequence
Nucleotide Mapping
Nucleic acid sequence
Lectin
Blood Proteins
DNA
Molecular biology
Killer Cells, Natural
Biochemistry
biology.protein
Electrophoresis, Polyacrylamide Gel
Proteoglycans
Asialoglycoprotein receptor
Subjects
Details
- ISSN :
- 01615890
- Volume :
- 29
- Database :
- OpenAIRE
- Journal :
- Molecular Immunology
- Accession number :
- edsair.doi.dedup.....32d5741b163b431a5bb459d5ab256d8e
- Full Text :
- https://doi.org/10.1016/0161-5890(92)90012-m