BIOMAT Database Logo BIOMAT Database Logo

Interaction of human serum proteinase inhibitors with proteolytic enzymes of animal, plant, and bacterial origin. 1974

M Sasaki, and H Yamamoto, and S Iida

UI MeSH Term Description Entries
D008259 Macroglobulins Serum globulins with high molecular weight. (Dorland, 28th ed)
D010447 Peptide Hydrolases Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES. Peptidase,Peptidases,Peptide Hydrolase,Protease,Proteases,Proteinase,Proteinases,Proteolytic Enzyme,Proteolytic Enzymes,Esteroproteases,Enzyme, Proteolytic,Hydrolase, 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
D011480 Protease Inhibitors Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES). Antiprotease,Endopeptidase Inhibitor,Endopeptidase Inhibitors,Peptidase Inhibitor,Peptidase Inhibitors,Peptide Hydrolase Inhibitor,Peptide Hydrolase Inhibitors,Peptide Peptidohydrolase Inhibitor,Peptide Peptidohydrolase Inhibitors,Protease Antagonist,Protease Antagonists,Antiproteases,Protease Inhibitor,Antagonist, Protease,Antagonists, Protease,Hydrolase Inhibitor, Peptide,Hydrolase Inhibitors, Peptide,Inhibitor, Endopeptidase,Inhibitor, Peptidase,Inhibitor, Peptide Hydrolase,Inhibitor, Peptide Peptidohydrolase,Inhibitor, Protease,Inhibitors, Endopeptidase,Inhibitors, Peptidase,Inhibitors, Peptide Hydrolase,Inhibitors, Peptide Peptidohydrolase,Inhibitors, Protease,Peptidohydrolase Inhibitor, Peptide,Peptidohydrolase Inhibitors, Peptide
D001798 Blood Proteins Proteins that are present in blood serum, including SERUM ALBUMIN; BLOOD COAGULATION FACTORS; and many other types of proteins. Blood Protein,Plasma Protein,Plasma Proteins,Serum Protein,Serum Proteins,Protein, Blood,Protein, Plasma,Protein, Serum,Proteins, Blood,Proteins, Plasma,Proteins, Serum
D001963 Bromelains Protein-digesting and milk-clotting enzymes found in PINEAPPLE fruit juice and stem tissue. Enzymes from the two sources are distinguished as fruit bromelain and stem bromelain. This enzyme was formerly listed as EC 3.4.22.4. Bromelins,Ananase,Bromelain,Bromelain-POS,Bromelin,Dayto Anase,Debrase,Dontisanin,Extranase,Mucozym,Proteozym,Traumanase,Bromelain POS,BromelainPOS
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
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
D004586 Electrophoresis An electrochemical process in which macromolecules or colloidal particles with a net electric charge migrate in a solution under the influence of an electric current. Electrophoreses
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man

Related Publications

M Sasaki, and H Yamamoto, and S Iida
Proteolytic enzymes and biological inhibitors. IV. Bacterial proteinase inhibitors and their effect upon enzymes of various origin.
January 1970, Acta pathologica et microbiologica Scandinavica. Section B: Microbiology and immunology,
M Sasaki, and H Yamamoto, and S Iida
Proteolytic enzymes and biological inhibitors. 3. Naturally occurring inhibitors in some animal and plant materials and their effect upon proteolytic enzymes of various origin.
January 1970, Acta pathologica et microbiologica Scandinavica. Section B: Microbiology and immunology,
M Sasaki, and H Yamamoto, and S Iida
Plant inhibitors of proteolytic enzymes.
January 1984, Die Nahrung,
M Sasaki, and H Yamamoto, and S Iida
Soybean proteinase inhibitors and human proteolytic enzymes: selective inactivation of inhibitors by treatment with human gastric juice.
December 1981, The Journal of nutrition,
M Sasaki, and H Yamamoto, and S Iida
[Cysteine proteinase inhibitors of animal origin].
July 1989, Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme,
M Sasaki, and H Yamamoto, and S Iida
Proteolytic enzymes and biological inhibitors. VI. Antibodies in animal sera against the proteinase of Corynebacterium pyogenes.
January 1971, Acta pathologica et microbiologica Scandinavica. Section B: Microbiology and immunology,
M Sasaki, and H Yamamoto, and S Iida
Elastases from human and canine granulocytes, II. Interaction with protease inhibitors of animal, plant, and microbial origin.
January 1977, Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
M Sasaki, and H Yamamoto, and S Iida
[Proteolytic enzymes of blood serum and their inhibitors].
February 1952, Polski tygodnik lekarski,
M Sasaki, and H Yamamoto, and S Iida
Antifatty liver action of proteolytic enzymes of animal and plant origin in pancreatic duct-ligated rats.
September 1954, Gastroenterology,
M Sasaki, and H Yamamoto, and S Iida
Proteolytic enzymes; further studies on protein, polypeptide, and other inhibitors of serum proteinase, leucoproteinase, trypsin, and papain.
November 1949, The Journal of general physiology,
Copied contents to your clipboard!