Primary Structure and Functional Expression of Heavy- and Light-Chain Variable Region Genes of a Monoclonal Antibody Specific for Human Fibrin

Hybridoma ◽  
1997 ◽  
Vol 16 (3) ◽  
pp. 235-241 ◽  
Author(s):  
ZENGXUAN SONG ◽  
YINGLIN CAI ◽  
DANYING SONG ◽  
JING XU ◽  
HONGWEI YUAN ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Light Chain ◽  
Primary Structure ◽  
Variable Region ◽  
Functional Expression ◽  
Variable Region Genes

Molecular analysis of the murine lupus-associated anti-self response: involvement of a large number of heavy and light chain variable region genes

1987 ◽  
Vol 17 (1) ◽  
pp. 91-95 ◽  
Author(s):  
Reinhard Kofler ◽  
Daniel J. Noonan ◽  
Robert Strohal ◽  
Robert S. Balderas ◽  
Niels P. H. Moller ◽  
...  
Keyword(s):  
Molecular Analysis ◽  
Light Chain ◽  
Variable Region ◽  
Murine Lupus ◽  
Variable Region Genes

Construction and Expression of a Bifunctional Single-Chain Antibody against Bacillus cereusSpores

1998 ◽  
Vol 64 (7) ◽  
pp. 2490-2496 ◽  
Author(s):  
Kai Koo ◽  
Peggy M. Foegeding ◽  
Harold E. Swaisgood
Keyword(s):  
Monoclonal Antibody ◽  
Recombinant Antibody ◽  
Expression System ◽  
Variable Region ◽  
Hybridoma Cells ◽  
Antigen Specificity ◽  
Single Chain ◽  
Single Chain Antibody ◽  
Western Blots ◽  
Variable Region Genes

ABSTRACT The variable-region genes of monoclonal antibody againstBacillus cereus spores were cloned from mouse hybridoma cells by reverse transcription-PCR. The heavy- and light-chain variable-region genes were connected by a 45-base linker DNA to allow folding of the fusion protein into a functional tertiary structure. For detection of protein expression, a 10-amino-acid strep tag (biotin-like peptide) was attached to the C terminus of recombinant antibody as the reporter peptide. The single-chain antibody construct was inserted into the expression vector and expressed in Escherichia coliunder the control of the T7 RNA polymerase-T7 promoter expression system. The expressed single-chain antibody was detected on Western blots by using a streptavidin-conjugated enzyme system. This small recombinant antibody fragment (ca. 28,000 Da by calculation) hadB. cereus spore binding ability and antigen specificity similar to those of its parent native monoclonal antibody.

Polymemse Chain Reaction Using Mixed Primers: Cloning of Human Monoclonal Antibody Variable Region Genes from Single Hybridoma Cells

1989 ◽  
Vol 7 (9) ◽  
pp. 934-938 ◽  
Author(s):  
James W. Larrick ◽  
Lena Danielsson ◽  
Carol A. Brenner ◽  
Ellen F. Wallace ◽  
Magnus Abrahamson ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Human Monoclonal Antibody ◽  
Variable Region ◽  
Hybridoma Cells ◽  
Chain Reaction ◽  
Variable Region Genes

scholarly journals The primary structure of the variable region of an immunoglobin IV light-chain amyloid-fibril protein (AL GIL)

1988 ◽  
Vol 256 (3) ◽  
pp. 973-980 ◽  
Author(s):  
E M Fykse ◽  
K Sletten ◽  
G Husby ◽  
G G Cornwell
Keyword(s):  
Amino Acid ◽  
Light Chain ◽  
Primary Structure ◽  
Amyloid Fibril ◽  
Variable Region ◽  
Acceptor Site ◽  
Amino Acid Residues ◽  
Bence Jones Protein ◽  
Sequence Homologies ◽  
Amyloid Fibril Protein

The primary structure of the variable region of an amyloid-fibril protein GIL of immunoglobulin lambda-light-chain origin (AL) was determined. The AL protein obtained from the fibrils in the spleen of a 54-year-old man with primary systemic amyloidosis could be assigned to subgroup IV of the lambda variable-region sequence. About 50% of the protein was found to be truncated in the N-terminus and lacked the first six amino acid residues. The polypeptides consisted of about 146 amino acid residues and contained traces of carbohydrate. An acceptor site for N-glycosylation was found in positions 90-93, but no glycopeptide could be isolated. Comparison of the amino acid sequence of AL protein GIL with that of the only Bence-Jones protein of subgroup IV previously studied revealed a sequence homology of 89%. A similar comparison made with other AL proteins gave sequence homologies below 66%.

Sign in / Sign up

Export Citation Format

Share Document