High-level production of biologically active human alpha 1-antitrypsin in Escherichia coli. 1984

M Courtney, and A Buchwalder, and L H Tessier, and M Jaye, and A Benavente, and A Balland, and V Kohli, and R Lathe, and P Tolstoshev, and J P Lecocq

A cDNA clone containing the complete human alpha 1-antitrypsin sequence was isolated from a human liver cDNA bank by screening with a chemically synthesized oligonucleotide probe. DNA sequences encoding the alpha 1-antitrypsin mature polypeptide were inserted into an Escherichia coli expression vector that allows transcription from the efficient leftward promoter of bacteriophage lambda (PL) and initiation of translation at the lambda cII gene ribosome-binding site. This construction resulted in the induction of a 45-kilodalton protein at a level of approximately 15% of total cell protein. The polypeptide produced was recognized by antisera raised against human alpha 1-antitrypsin protein and displayed normal biological activity in an in vitro antielastase assay.

UI MeSH Term Description Entries
D010196 Pancreatic Elastase A protease of broad specificity, obtained from dried pancreas. Molecular weight is approximately 25,000. The enzyme breaks down elastin, the specific protein of elastic fibers, and digests other proteins such as fibrin, hemoglobin, and albumin. EC 3.4.21.36. Elastase,Pancreatopeptidase,Elastase I,Pancreatic Elastase I,Elastase I, Pancreatic,Elastase, Pancreatic
D010957 Plasmids Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS. Episomes,Episome,Plasmid
D003001 Cloning, Molecular The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells. Molecular Cloning
D004247 DNA A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine). DNA, Double-Stranded,Deoxyribonucleic Acid,ds-DNA,DNA, Double Stranded,Double-Stranded DNA,ds DNA
D004262 DNA Restriction Enzymes Enzymes that are part of the restriction-modification systems. They catalyze the endonucleolytic cleavage of DNA sequences which lack the species-specific methylation pattern in the host cell's DNA. Cleavage yields random or specific double-stranded fragments with terminal 5'-phosphates. The function of restriction enzymes is to destroy any foreign DNA that invades the host cell. Most have been studied in bacterial systems, but a few have been found in eukaryotic organisms. They are also used as tools for the systematic dissection and mapping of chromosomes, in the determination of base sequences of DNAs, and have made it possible to splice and recombine genes from one organism into the genome of another. EC 3.21.1. Restriction Endonucleases,DNA Restriction Enzyme,Restriction Endonuclease,Endonuclease, Restriction,Endonucleases, Restriction,Enzymes, DNA Restriction,Restriction Enzyme, DNA,Restriction Enzymes, DNA
D004926 Escherichia coli A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000515 alpha 1-Antitrypsin Plasma glycoprotein member of the serpin superfamily which inhibits TRYPSIN; NEUTROPHIL ELASTASE; and other PROTEOLYTIC ENZYMES. Trypsin Inhibitor, alpha 1-Antitrypsin,alpha 1-Protease Inhibitor,alpha 1-Proteinase Inhibitor,A1PI,Prolastin,Serpin A1,Zemaira,alpha 1 Antiprotease,alpha 1-Antiproteinase,1-Antiproteinase, alpha,Antiprotease, alpha 1,Inhibitor, alpha 1-Protease,Inhibitor, alpha 1-Proteinase,Trypsin Inhibitor, alpha 1 Antitrypsin,alpha 1 Antiproteinase,alpha 1 Antitrypsin,alpha 1 Protease Inhibitor,alpha 1 Proteinase Inhibitor
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001483 Base Sequence The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence. DNA Sequence,Nucleotide Sequence,RNA Sequence,DNA Sequences,Base Sequences,Nucleotide Sequences,RNA Sequences,Sequence, Base,Sequence, DNA,Sequence, Nucleotide,Sequence, RNA,Sequences, Base,Sequences, DNA,Sequences, Nucleotide,Sequences, RNA

Related Publications

M Courtney, and A Buchwalder, and L H Tessier, and M Jaye, and A Benavente, and A Balland, and V Kohli, and R Lathe, and P Tolstoshev, and J P Lecocq
October 1987, Molecular biology & medicine,
M Courtney, and A Buchwalder, and L H Tessier, and M Jaye, and A Benavente, and A Balland, and V Kohli, and R Lathe, and P Tolstoshev, and J P Lecocq
July 1990, Proceedings of the National Academy of Sciences of the United States of America,
M Courtney, and A Buchwalder, and L H Tessier, and M Jaye, and A Benavente, and A Balland, and V Kohli, and R Lathe, and P Tolstoshev, and J P Lecocq
November 2018, Protein expression and purification,
M Courtney, and A Buchwalder, and L H Tessier, and M Jaye, and A Benavente, and A Balland, and V Kohli, and R Lathe, and P Tolstoshev, and J P Lecocq
November 1995, Gene,
M Courtney, and A Buchwalder, and L H Tessier, and M Jaye, and A Benavente, and A Balland, and V Kohli, and R Lathe, and P Tolstoshev, and J P Lecocq
December 1990, Gene,
M Courtney, and A Buchwalder, and L H Tessier, and M Jaye, and A Benavente, and A Balland, and V Kohli, and R Lathe, and P Tolstoshev, and J P Lecocq
December 1992, Gene,
M Courtney, and A Buchwalder, and L H Tessier, and M Jaye, and A Benavente, and A Balland, and V Kohli, and R Lathe, and P Tolstoshev, and J P Lecocq
January 1984, FEBS letters,
M Courtney, and A Buchwalder, and L H Tessier, and M Jaye, and A Benavente, and A Balland, and V Kohli, and R Lathe, and P Tolstoshev, and J P Lecocq
October 1991, Molecular and cellular endocrinology,
M Courtney, and A Buchwalder, and L H Tessier, and M Jaye, and A Benavente, and A Balland, and V Kohli, and R Lathe, and P Tolstoshev, and J P Lecocq
January 1992, International journal of peptide and protein research,
M Courtney, and A Buchwalder, and L H Tessier, and M Jaye, and A Benavente, and A Balland, and V Kohli, and R Lathe, and P Tolstoshev, and J P Lecocq
January 2017, Methods in molecular biology (Clifton, N.J.),
Copied contents to your clipboard!