[go: up one dir, main page]

Moore et al., 1986 - Google Patents

Purification of human collagenases with a hydroxamic acid affinity column

Moore et al., 1986

Document ID
13291193189058100323
Author
Moore W
Spilburg C
Publication year
Publication venue
Biochemistry

External Links

Snippet

Monsanto Company, St. Louis, Missouri 63198 Received January 16, 1986; Revised Manuscript Received March 20, 1986 abstract: Human collagenase has been isolated from skin fibroblasts and rheumatoid synovium by using an affinity matrix, prepared by coupling …
Continue reading at pubs.acs.org (other versions)

Classifications

    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50—Proteinases Endopeptidases (3.4.21-3.4.25)
    • C12N9/64—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
    • C12N9/6421—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
    • C12N9/6424—Serine endopeptidases (3.4.21)
    • C12N9/6427—Chymotrypsins (3.4.21.1; 3.4.21.2); Trypsin (3.4.21.4)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50—Proteinases Endopeptidases (3.4.21-3.4.25)
    • C12N9/52—Proteinases Endopeptidases (3.4.21-3.4.25) derived from bacteria
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/16—Hydrolases (3) acting on ester bonds (3.1)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES OR MICRO-ORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
    • C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions
    • C12Q1/34—Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions involving hydrolase
    • C12Q1/37—Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions involving hydrolase involving peptidase or proteinase
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
    • C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
    • C07K5/06—Dipeptides
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
    • C07K1/06—General 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
    • C07K1/061—General 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
Moore et al. Purification of human collagenases with a hydroxamic acid affinity column
Orlowski et al. Purification and specificity of a membrane-bound metalloendopeptidase from bovine pituitaries
Wilk et al. Cation‐sensitive neutral endopeptidase: isolation and specificity of the bovine pituitary enzyme
Smith et al. Pseudotrypsin: a modified bovine trypsin produced by limited autodigestion
Koida et al. Post-proline cleaving enzyme. Purification of this endopeptidase by affinity chromatography.
Kimmel et al. The properties of papain
Smyth [24] Techniques in enzymic hydrolysis
Orlowski et al. Evidence for the presence of five distinct proteolytic components in the pituitary multicatalytic proteinase complex. Properties of two components cleaving bonds on the carboxyl side of branched chain and small neutral amino acids
Maroux et al. Purification and specificity of porcine enterokinase
McRae et al. Mapping the active sites of bovine thrombin, factor IXa, factor Xa, factor XIa, factor XIIa, plasma kallikrein, and trypsin with amino acid and peptide thioesters: development of new sensitive substrates
Simmons et al. Membrane-bound aminopeptidase P from bovine lung. Its purification, properties, and degradation of bradykinin.
Kobayashi et al. Acyl-peptide hydrolase from rat liver. Characterization of enzyme reaction.
Rasnick et al. Active site directed irreversible inhibition of thermolysin
Ota et al. Enzymatic methylation of L-isoaspartyl residues derived from aspartyl residues in affinity-purified calmodulin: the role of conformational flexibility in spontaneous isoaspartyl formation
Tsu et al. The substrate specificity of Uca pugilator collagenolytic serine protease 1 correlates with the bovine type I collagen cleavage sites.
Marinkovic et al. Purification of carboxypeptidase B from human pancreas
Breddam Chemically modified carboxypeptidase Y with increased amidase activity
Pedersen et al. Amino‐Acid Sequence of the Peptide Segment Liberated during Activation of Prochymosin (Prorennin)
Moore et al. Peptide hydroxamic acids inhibit skin collagenase
Iio et al. Specificity of acid proteinase A from Aspergillus niger var. macrosporus towards B-chain of performic acid oxidized bovine insulin
Baratti et al. On the catalytic and binding sites of porcine enteropeptidase
Simmons et al. Carboxamidopeptidase: purification and characterization of a neurohypophyseal hormone inactivating peptidase from toad skin
Bensusan Investigation of the products of an enzymic hydrolysis of collagens
Green et al. A prolyl endopeptidase from murine macrophages, its assay and specific inactivation
Rush et al. Fluorogenic substrates for the enkephalin-degrading neutral endopeptidase (Enkephalinase)