[go: up one dir, main page]
More Web Proxy on the site http://driver.im/

Oka et al., 1970 - Google Patents

Specificity of pepsin: Size and property of the active site

Oka et al., 1970

View PDF @Full View
Document ID
2202261845669086385
Author
Oka T
Morihara K
Publication year
Publication venue
FEBS letters

External Links

Snippet

The method of measuring the size of an enzyme's active site by presenting it with substrates large enough to show up interactions with further-most parts of the site was first applied to papain by Schechter and Berger [1]. The active site there was found to cover 25 A …
Continue reading at core.ac.uk (PDF) (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)
    • C12N9/52Proteinases Endopeptidases (3.4.21-3.4.25) derived from bacteria

Similar Documents

Publication Publication Date Title
Püschel et al. Isolation and characterization of dipeptidyl peptidase IV from human placenta
Orlowski et al. Purification and specificity of a membrane-bound metalloendopeptidase from bovine pituitaries
Morihara et al. Thermolysin: kinetic study with oligopeptides
Del Mar et al. Substrate specificity of human pancreatic elastase 2
Masaki et al. A new proteolytic enzyme from Achromobacter lyticus M497-1
Oka et al. Trypsin as a catalyst for peptide synthesis
Morihara et al. Subtilisin BPN′: Kinetic study with oligopeptides
Morihara et al. Specificity of proteinase K from Tritirachium album Limber for synthetic peptides
Maita et al. Amino‐acid sequence of the L‐1 light chain of chicken cardiac‐muscle myosin
Tong et al. Hypodermin A, a trypsin-like neutral proteinase from the insect Hypoderma lineatum
HIRAO et al. Purification and characterization of a calcium-activated neutral protease from monkey brain and its action on neuropeptides
Oka et al. Specificity of pepsin: Size and property of the active site
Feracci et al. Enzymatic and immunological properties of the protease form of aminopeptidases N and A from pig and rabbit intestinal brush border
Sengupta et al. Comparative studies on calotropins DI and DII from the latex of Calotropis gigantea
Morihara et al. On the specificity of Pseudomonas aeruginosa alkaline proteinase with synthetic peptides
Schenkein et al. Proteases from mouse submaxillary gland
Kessler et al. A novel aminopeptidase from Clostridium histolyticum
Morihara et al. Comparison of various types of subtilisins: size and properties of the active site
Nakadai et al. Purification and properties of acid carboxypeptidase I from Aspergillus oryzae
Morihara et al. Pepstatin-Insensitive Acid Proteases from Scytalidium lignicolum: Kinetic Study with Synthetic Peptides
Oka et al. On the specificity of a rennin-like enzyme from Mucor pusillus
Williams et al. Hydrolysis of peptide bonds of the oxidized B-chain of insulin by Endothia parasitica protease
Morihara et al. Comparative study of various serine proteinases from microorganisms: specificity with oligopeptides
Oka et al. Comparative specificity of microbial acid proteinases for synthetic peptides: II. Effect of secondary interaction
Morihara et al. Effect of secondary interaction on the enzymatic activity of trypsin-like enzymes from Streptomyces