BIOMAT Database Logo BIOMAT Database Logo

Interchain disulfide bonds and subunit organization in human serum cholinesterase. 1979

O Lockridge, and H W Eckerson, and B N La Du

UI MeSH Term Description Entries
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D002802 Cholinesterases Acylcholineacylhydrolase,Cholase,Cholinesterase
D004220 Disulfides Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties. Disulfide
D004355 Drug Stability The chemical and physical integrity of a pharmaceutical product. Drug Shelf Life,Drugs Shelf Lives,Shelf Life, Drugs,Drug Stabilities,Drugs Shelf Life,Drugs Shelf Live,Life, Drugs Shelf,Shelf Life, Drug,Shelf Live, Drugs,Shelf Lives, Drugs
D004591 Electrophoresis, Polyacrylamide Gel Electrophoresis in which a polyacrylamide gel is used as the diffusion medium. Polyacrylamide Gel Electrophoresis,SDS-PAGE,Sodium Dodecyl Sulfate-PAGE,Gel Electrophoresis, Polyacrylamide,SDS PAGE,Sodium Dodecyl Sulfate PAGE,Sodium Dodecyl Sulfate-PAGEs
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D046911 Macromolecular Substances Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure. Macromolecular Complexes,Macromolecular Compounds,Macromolecular Compounds and Complexes,Complexes, Macromolecular,Compounds, Macromolecular,Substances, Macromolecular

Related Publications

O Lockridge, and H W Eckerson, and B N La Du
The interchain disulfide bonds of a human pathological immunoglobulin.
December 1967, Biochemistry,
O Lockridge, and H W Eckerson, and B N La Du
Location of disulfide bonds within the sequence of human serum cholinesterase.
September 1987, The Journal of biological chemistry,
O Lockridge, and H W Eckerson, and B N La Du
Interchain disulfide bonds in crotamine self-association.
June 1990, Journal of biochemistry,
O Lockridge, and H W Eckerson, and B N La Du
Relative labilities of interchain disulfide bonds in human immunoglobulin M subunits.
February 1970, Biochemistry,
O Lockridge, and H W Eckerson, and B N La Du
Interchain disulfide bonds of goat immunoglobulin G.
June 1971, Biochemistry,
O Lockridge, and H W Eckerson, and B N La Du
Isolation of the monomeric subunit of immunoglobulin M with its interchain disulfide bonds intact.
August 1968, Biochemistry,
O Lockridge, and H W Eckerson, and B N La Du
Identification of the interchain disulfide bonds of dimeric human placental lactogen.
May 1979, The Journal of biological chemistry,
O Lockridge, and H W Eckerson, and B N La Du
Mouse monoclonal IgA antibodies lack interchain disulfide bonds.
January 1995, Archivum immunologiae et therapiae experimentalis,
O Lockridge, and H W Eckerson, and B N La Du
Role of interchain disulfide bonds on the assembly and secretion of human fibrinogen.
January 1994, The Journal of biological chemistry,
O Lockridge, and H W Eckerson, and B N La Du
Loss of the interchain disulfide peptide and dissociation of the tetramer following limited proteolysis of native human serum cholinesterase.
October 1982, The Journal of biological chemistry,
Copied contents to your clipboard!