The amino acid sequence of a carboxypeptidase inhibitor from potatoes. 1975

G M Hass, and H Nau, and K Biemann, and D T Grahn, and L H Ericsson, and H Neurath

The carboxypeptidase inhibitor from Russet Burbank potatoes (C. A. Ryan et al. (1974b), J. Biol. Chem 249, 5495) is a mixture of approximately equal amounts of two polypeptide chains containing 38 and 39 amino acid residues, respectively. The chains differ in their amino terminal sequence only, one beginning with smaller than Glu-His-Ala ... and the other with smaller than Glu-Gln-His-Ala ..... Specific cleavage procedures utilized in determining the complete amino acid sequence of the inhibitor included acid cleavage of the aspartyl-proline bond and tryptic and chymotryptic digestion. Mass spectrometry, automatic Edman degradation, and subtractive Edman degradation were employed in sequencing the resulting peptide fragments.

UI MeSH Term Description Entries
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D010944 Plants Multicellular, eukaryotic life forms of kingdom Plantae. Plants acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations. It is a non-taxonomical term most often referring to LAND PLANTS. In broad sense it includes RHODOPHYTA and GLAUCOPHYTA along with VIRIDIPLANTAE. Plant
D002268 Carboxypeptidases Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue. Carboxypeptidase
D002621 Chemistry A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.
D002918 Chymotrypsin A serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN. It selectively cleaves aromatic amino acids on the carboxyl side. Alpha-Chymotrypsin Choay,Alphacutanée,Avazyme
D004791 Enzyme Inhibitors Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction. Enzyme Inhibitor,Inhibitor, Enzyme,Inhibitors, Enzyme
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
D000596 Amino Acids Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins. Amino Acid,Acid, Amino,Acids, Amino
D013058 Mass Spectrometry An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers. Mass Spectroscopy,Spectrometry, Mass,Spectroscopy, Mass,Spectrum Analysis, Mass,Analysis, Mass Spectrum,Mass Spectrum Analysis,Analyses, Mass Spectrum,Mass Spectrum Analyses,Spectrum Analyses, Mass
D013861 Thiocyanates Organic derivatives of thiocyanic acid which contain the general formula R-SCN. Rhodanate,Rhodanates

Related Publications

G M Hass, and H Nau, and K Biemann, and D T Grahn, and L H Ericsson, and H Neurath
April 1981, Biochemistry,
G M Hass, and H Nau, and K Biemann, and D T Grahn, and L H Ericsson, and H Neurath
January 1974, The Biochemical journal,
G M Hass, and H Nau, and K Biemann, and D T Grahn, and L H Ericsson, and H Neurath
December 1980, Biochemical and biophysical research communications,
G M Hass, and H Nau, and K Biemann, and D T Grahn, and L H Ericsson, and H Neurath
June 1976, Biochemistry,
G M Hass, and H Nau, and K Biemann, and D T Grahn, and L H Ericsson, and H Neurath
April 1981, Plant physiology,
G M Hass, and H Nau, and K Biemann, and D T Grahn, and L H Ericsson, and H Neurath
September 1974, The Journal of biological chemistry,
G M Hass, and H Nau, and K Biemann, and D T Grahn, and L H Ericsson, and H Neurath
August 1969, Proceedings of the National Academy of Sciences of the United States of America,
G M Hass, and H Nau, and K Biemann, and D T Grahn, and L H Ericsson, and H Neurath
June 1990, Journal of biochemistry,
G M Hass, and H Nau, and K Biemann, and D T Grahn, and L H Ericsson, and H Neurath
September 1969, Biochemistry,
G M Hass, and H Nau, and K Biemann, and D T Grahn, and L H Ericsson, and H Neurath
May 1975, Proceedings of the National Academy of Sciences of the United States of America,
Copied contents to your clipboard!