Nucleotide sequences of immunoglobulin mu heavy chain deletion mutants. 1983

W O Baczynsky, and S Sugii, and H Murialdo, and N Pennell, and C Filkin, and N Hozumi, and M J Shulman

Mutants of an IgM producing hybridoma cell line were isolated which produce mu heavy chain fragments. Two such mutants were found to have internal deletions in the mu gene and the nucleotide sequence of the deletion endpoints was determined. No evidence was found for a role of the heavy chain switch region in the formation of these deletions. The implications of these mutants in defining the requirements of immunoglobulin gene expression are discussed.

UI MeSH Term Description Entries
D007075 Immunoglobulin M A class of immunoglobulin bearing mu chains (IMMUNOGLOBULIN MU-CHAINS). IgM can fix COMPLEMENT. The name comes from its high molecular weight and originally was called a macroglobulin. Gamma Globulin, 19S,IgM,IgM Antibody,IgM1,IgM2,19S Gamma Globulin,Antibody, IgM
D007127 Immunoglobulin Constant Regions The domains of the immunoglobulin molecules that are invariable in their amino acid sequence within any class or subclass of immunoglobulin. They confer biological as well as structural functions to immunoglobulins. One each on both the light chains and the heavy chains comprises the C-terminus half of the IMMUNOGLOBULIN FAB FRAGMENT and two or three of them make up the rest of the heavy chains (all of the IMMUNOGLOBULIN FC FRAGMENT) Ig Constant Regions,Immunoglobulin Constant Region,Constant Region, Ig,Constant Region, Immunoglobulin,Constant Regions, Ig,Constant Regions, Immunoglobulin,Regions, Ig Constant
D007143 Immunoglobulin Heavy Chains The largest of polypeptide chains comprising immunoglobulins. They contain 450 to 600 amino acid residues per chain, and have molecular weights of 51-72 kDa. Immunoglobulins, Heavy-Chain,Heavy-Chain Immunoglobulins,Ig Heavy Chains,Immunoglobulin Heavy Chain,Immunoglobulin Heavy Chain Subgroup VH-I,Immunoglobulin Heavy Chain Subgroup VH-III,Heavy Chain Immunoglobulins,Heavy Chain, Immunoglobulin,Heavy Chains, Ig,Heavy Chains, Immunoglobulin,Immunoglobulin Heavy Chain Subgroup VH I,Immunoglobulin Heavy Chain Subgroup VH III,Immunoglobulins, Heavy Chain
D007148 Immunoglobulin mu-Chains The class of heavy chains found in IMMUNOGLOBULIN M. They have a molecular weight of approximately 72 kDa and they contain about 57 amino acid residues arranged in five domains and have more oligosaccharide branches and a higher carbohydrate content than the heavy chains of IMMUNOGLOBULIN G. Ig mu Chains,Immunoglobulins, mu-Chain,Immunoglobulin mu-Chain,mu Immunoglobulin Heavy Chain,mu Immunoglobulin Heavy Chains,mu-Chain Immunoglobulins,Chains, Ig mu,Immunoglobulin mu Chain,Immunoglobulin mu Chains,Immunoglobulins, mu Chain,mu Chain Immunoglobulins,mu Chains, Ig,mu-Chain, Immunoglobulin,mu-Chains, Immunoglobulin
D009154 Mutation Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations. Mutations
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
D002872 Chromosome Deletion Actual loss of portion of a chromosome. Monosomy, Partial,Partial Monosomy,Deletion, Chromosome,Deletions, Chromosome,Monosomies, Partial,Partial Monosomies
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
D006825 Hybridomas Cells artificially created by fusion of activated lymphocytes with neoplastic cells. The resulting hybrid cells are cloned and produce pure MONOCLONAL ANTIBODIES or T-cell products, identical to those produced by the immunologically competent parent cell. Hybridoma

Related Publications

W O Baczynsky, and S Sugii, and H Murialdo, and N Pennell, and C Filkin, and N Hozumi, and M J Shulman
April 1979, Journal of immunology (Baltimore, Md. : 1950),
W O Baczynsky, and S Sugii, and H Murialdo, and N Pennell, and C Filkin, and N Hozumi, and M J Shulman
October 1979, Nature,
W O Baczynsky, and S Sugii, and H Murialdo, and N Pennell, and C Filkin, and N Hozumi, and M J Shulman
January 1983, Nature,
W O Baczynsky, and S Sugii, and H Murialdo, and N Pennell, and C Filkin, and N Hozumi, and M J Shulman
September 1980, Nucleic acids research,
W O Baczynsky, and S Sugii, and H Murialdo, and N Pennell, and C Filkin, and N Hozumi, and M J Shulman
August 1983, Nucleic acids research,
W O Baczynsky, and S Sugii, and H Murialdo, and N Pennell, and C Filkin, and N Hozumi, and M J Shulman
July 1987, Nucleic acids research,
W O Baczynsky, and S Sugii, and H Murialdo, and N Pennell, and C Filkin, and N Hozumi, and M J Shulman
February 1993, The Journal of experimental medicine,
W O Baczynsky, and S Sugii, and H Murialdo, and N Pennell, and C Filkin, and N Hozumi, and M J Shulman
June 1980, Proceedings of the National Academy of Sciences of the United States of America,
W O Baczynsky, and S Sugii, and H Murialdo, and N Pennell, and C Filkin, and N Hozumi, and M J Shulman
July 1993, Somatic cell and molecular genetics,
W O Baczynsky, and S Sugii, and H Murialdo, and N Pennell, and C Filkin, and N Hozumi, and M J Shulman
August 1970, Science (New York, N.Y.),
Copied contents to your clipboard!