[go: up one dir, main page]

Favel et al., 1989 - Google Patents

Protease inhibitors from Ecballium elaterium seeds

Favel et al., 1989

Document ID
13376477518837722415
Author
Favel A
Mattras H
Coletti‐Previero M
Zwilling R
Robinson E
Castro B
Publication year
Publication venue
International journal of peptide and protein research

External Links

Snippet

Several protease inhibitors were found in the seeds of a Cucurbitacea, Ecballium elaterium, and were separated from one another by affinity and molecular sieve chromatography. Three main trypsin iso‐inhibitors were purified by ion‐exchange chromatography and the …
Continue reading at onlinelibrary.wiley.com (other versions)

Classifications

    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/48Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50Proteinases Endopeptidases (3.4.21-3.4.25)
    • C12N9/64Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
    • C12N9/6421Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
    • C12N9/6424Serine endopeptidases (3.4.21)
    • C12N9/6427Chymotrypsins (3.4.21.1; 3.4.21.2); Trypsin (3.4.21.4)
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/48Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50Proteinases Endopeptidases (3.4.21-3.4.25)
    • C12N9/52Proteinases Endopeptidases (3.4.21-3.4.25) derived from bacteria
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K14/00Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/81Protease inhibitors
    • C07K14/8107Endopeptidase (E.C. 3.4.21-99) inhibitors
    • C07K14/811Serine protease (E.C. 3.4.21) inhibitors
    • C07K14/8114Kunitz type inhibitors
    • C07K14/8117Bovine/basic pancreatic trypsin inhibitor (BPTI, aprotinin)
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K14/00Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/81Protease inhibitors
    • C07K14/815Protease inhibitors from leeches, e.g. hirudin, eglin
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K14/00Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/46Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K1/00General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
    • C07K1/06General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length using protecting groups or activating agents
    • C07K1/061General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length using protecting groups or activating agents using protecting groups

Similar Documents

Publication Publication Date Title
Favel et al. Protease inhibitors from Ecballium elaterium seeds
Jones et al. Properties of chromatographically purified trypsin inhibitors from lima beans
Kido et al. Kunitz-type protease inhibitor found in rat mast cells. Purification, properties, and amino acid sequence.
Vernon et al. A toxic thionin from Pyrularia pubera: purification, properties, and amino acid sequence
Wilson et al. The partial amino acid sequence of trypsin inhibitor II from garden bean, Phaseolus vulgaris, with location of the trypsin and elastase-reactive sites
Krishnamoorthi et al. A new protein inhibitor of trypsin and activated Hageman factor from pumpkin (Cucurbita maxima) seeds
Macedo et al. Trypsin inhibitor from Dimorphandra mollis seeds: purification and properties
Benson et al. Non-heme Iron Proteins: X. The Amino Acid Sequences of Ferredoxins from Leucaena Glauca
Kageyama et al. Purification and characterization of a cysteine proteinase from silkworm eggs
Griffith et al. Structural evidence for leucine at the reactive site of heparin cofactor II
Belozersky et al. Isolation and properties of a metalloproteinase from buckwheat (Fagopyrum esculentum) seeds
Lin et al. Trypsin inhibitor from the seeds of Acacia confusa
Mikola Germinating barley grains contain five acid carboxypeptidases with complementary substrate specificities
Odani et al. Proteinase Inhibators from a Mimosoideae Legume
Yoshida et al. Purification and characterization of an acidic amino acid specific endopeptidase of Streptomyces griseus obtained from a commercial preparation (Pronase)
Tanaka et al. Purification and primary structure determination of a Bowman-Birk trypsin inhibitor from Torresea cearensis seeds
Maeda The complete amino-acid sequence of the endogenous α-amylase inhibitor in wheat
Dopheide et al. Studies on the tryptophan residues in porcine pepsin
Huang et al. Isolation of a trypsin inhibitor with deletion of N-terminal pentapeptide from the seeds of Momordica cochinchinensis, the Chinese drug mubiezhi
Ramage et al. Solid phase peptide synthesis of ubiquitin
Benkouka et al. Porcine pancreatic lipase: The disulfide bridges and the sulfhydryl groups
Joubert et al. The primary structure of the inhibitor of tissue plasminogen activator found in the seeds of Erythrina caffra
Haldar et al. Trypsin inhibitors from ridged gourd (Luffa acutangula Linn.) seeds: purification, properties, and amino acid sequences
Tashiro et al. The complete amino acid sequence of a major trypsin inhibitor from seeds of foxtail millet (Setaria italica)
Sakato et al. Broad‐Specificity Proteinase Inhibitors in Scopolia japonica (Solanaceae) Cultured Cells: Isolation, Physicochemical Properties, and Inhibition Kinetics