Expression and characterization of a B cell growth promoting polypeptide derived from the 12 kDa B cell growth factor gene ( BCGF 1)

The expression and partial purification of recombinant 12 kDa B cell growth factor are reported. The polypeptide was derived from the genomic sequence of the gene ( BCGF 1) which is here shown to be a single copy gene that localizes to human chromosome 16. When expressed as a glutathione S-transfera...

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Bibliographic Details
Published in:FEBS letters 1995-03, Vol.361 (2), p.233-237
Main Authors: Kovanen, Panu E., Virtaneva, Kimmo, Harju, Leena, Kantor, Carmela, Gahmberg, Carl G., Timonen, Tuomo
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
B cell growth factor
B cell proliferation
B-Lymphocytes - drug effects
B-Lymphocytes - immunology
Base Sequence
BCGF
BCGF 1
Binding Sites
Blotting, Southern
Blotting, Western
Cells, Cultured
Chromosome 16
Chromosome Mapping
Chromosomes, Human, Pair 16
DNA - blood
DNA - isolation & purification
DNA Primers
Gene
Gene Expression
glutathione S-transferase
Glutathione Transferase - biosynthesis
GST
Humans
Hybrid Cells
Interleukin-4 - biosynthesis
Interleukin-4 - genetics
Interleukin-4 - pharmacology
Leukocytes - metabolism
Lymphocyte Activation
Molecular Sequence Data
Molecular Weight
Peptides - chemical synthesis
Peptides - chemistry
Peptides - immunology
Polymerase Chain Reaction
Recombinant 12 kDa BCGF
Recombinant Fusion Proteins - biosynthesis
Recombinant Proteins - pharmacology
Restriction Mapping
Rodentia
Sequence Homology, Amino Acid
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Description
Summary:The expression and partial purification of recombinant 12 kDa B cell growth factor are reported. The polypeptide was derived from the genomic sequence of the gene ( BCGF 1) which is here shown to be a single copy gene that localizes to human chromosome 16. When expressed as a glutathione S-transferase fusion protein in E. coli, the protein appears as a 38 kDa polypeptide in Western blot analysis using a peptide antibody. The purified fusion protein stimulates the proliferation of activated human B cells in a dose-dependent manner, and the active site resides within the 104 carboxy-terminal amino acids. The availability of biologically active recombinant 12 kDa B cell growth factor will enable its evaluation in B cell growth regulation, and provides a new means of in vitro culturing of human B lymphocytes.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(95)00186-D