Serine at the active center of yeast carboxypeptidase. 1973

R Hayashi, and S Moore, and W H Stein

UI MeSH Term Description Entries
D007461 Iodoacetates Iodinated derivatives of acetic acid. Iodoacetates are commonly used as alkylating sulfhydryl reagents and enzyme inhibitors in biochemical research. Iodoacetic Acids,Acids, Iodoacetic
D007531 Isoflurophate A di-isopropyl-fluorophosphate which is an irreversible cholinesterase inhibitor used to investigate the NERVOUS SYSTEM. DFP,Diisopropylfluorophosphate,Fluostigmine,Bis(1-methylethyl) Phosphorofluoridate,Di-isopropylphosphorofluoridate,Diisopropylphosphofluoridate,Dyflos,Floropryl,Fluorostigmine,Di isopropylphosphorofluoridate
D010434 Pepsin A Formed from pig pepsinogen by cleavage of one peptide bond. The enzyme is a single polypeptide chain and is inhibited by methyl 2-diaazoacetamidohexanoate. It cleaves peptides preferentially at the carbonyl linkages of phenylalanine or leucine and acts as the principal digestive enzyme of gastric juice. Pepsin,Pepsin 1,Pepsin 3
D010450 Endopeptidases A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS. Endopeptidase,Peptide Peptidohydrolases
D010748 Phosphopeptides PEPTIDES that incorporate a phosphate group via PHOSPHORYLATION. Phosphopeptide
D010750 Phosphoproteins Phosphoprotein
D010761 Phosphorus Radioisotopes Unstable isotopes of phosphorus that decay or disintegrate emitting radiation. P atoms with atomic weights 28-34 except 31 are radioactive phosphorus isotopes. Radioisotopes, Phosphorus
D011489 Protein Denaturation Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein. Denaturation, Protein,Denaturations, Protein,Protein Denaturations
D002268 Carboxypeptidases Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue. Carboxypeptidase
D002850 Chromatography, Gel Chromatography on non-ionic gels without regard to the mechanism of solute discrimination. Chromatography, Exclusion,Chromatography, Gel Permeation,Chromatography, Molecular Sieve,Gel Filtration,Gel Filtration Chromatography,Chromatography, Size Exclusion,Exclusion Chromatography,Gel Chromatography,Gel Permeation Chromatography,Molecular Sieve Chromatography,Chromatography, Gel Filtration,Exclusion Chromatography, Size,Filtration Chromatography, Gel,Filtration, Gel,Sieve Chromatography, Molecular,Size Exclusion Chromatography

Related Publications

R Hayashi, and S Moore, and W H Stein
September 1994, Biochemistry,
R Hayashi, and S Moore, and W H Stein
January 1964, Federation proceedings,
R Hayashi, and S Moore, and W H Stein
April 1966, The Journal of biological chemistry,
R Hayashi, and S Moore, and W H Stein
December 1972, The Journal of biological chemistry,
R Hayashi, and S Moore, and W H Stein
October 1969, The Journal of biological chemistry,
R Hayashi, and S Moore, and W H Stein
May 1971, The Journal of biological chemistry,
R Hayashi, and S Moore, and W H Stein
October 2005, The Journal of biological chemistry,
R Hayashi, and S Moore, and W H Stein
January 1971, European journal of biochemistry,
R Hayashi, and S Moore, and W H Stein
March 2004, Phytochemistry,
R Hayashi, and S Moore, and W H Stein
May 1982, International journal of peptide and protein research,
Copied contents to your clipboard!