[go: up one dir, main page]

Andreasen et al., 1984 - Google Patents

Inactive proenzyme to tissue‐type plasminogen activator from human melanoma cells, identified after affinity purification with a monoclonal antibody.

Andreasen et al., 1984

View PDF
Document ID
10627578587652359526
Author
Andreasen P
Nielsen L
Grøndahl‐Hansen J
Skriver L
Zeuthen J
Stephens R
Danø K
Publication year
Publication venue
The EMBO Journal

External Links

Snippet

The human 66 000 mol. wt. plasminogen activator (HPA66; tissue‐type plasminogen activator) has been purified from melanoma cells by a one‐step affinity method with a monoclonal antibody. HPA66 purified in this way consists mainly of a one‐polypeptide chain …
Continue reading at www.embopress.org (PDF) (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)
    • C12N9/6456—Plasminogen activators
    • 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
    • C12Y—ENZYMES
    • C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
    • C12Y304/21—Serine endopeptidases (3.4.21)
    • C12Y304/21069—Protein C activated (3.4.21.69)
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
    • G01N2333/90—Enzymes; Proenzymes
    • G01N2333/914—Hydrolases (3)
    • G01N2333/948—Hydrolases (3) acting on peptide bonds (3.4)
    • G01N2333/95—Proteinases, i.e. endopeptidases (3.4.21-3.4.99)
    • G01N2333/964—Proteinases, i.e. endopeptidases (3.4.21-3.4.99) derived from animal tissue
    • G01N2333/96425—Proteinases, i.e. endopeptidases (3.4.21-3.4.99) derived from animal tissue from mammals
    • G01N2333/96427—Proteinases, i.e. endopeptidases (3.4.21-3.4.99) derived from animal tissue from mammals in general
    • 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
    • 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
    • C12Q1/56—Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions involving blood clotting factors, e.g. involving thrombin, thromboplastin, fibrinogen

Similar Documents

Publication Publication Date Title
Andreasen et al. Inactive proenzyme to tissue‐type plasminogen activator from human melanoma cells, identified after affinity purification with a monoclonal antibody.
Zamarron et al. Biological and thrombolytic properties of proenzyme and active forms of human urokinase–I. Fibrinolytic and fibrinogenolytic properties in human plasma in vitro of urokinases obtained from human urine or by recombinant DNA technology
Andreasen et al. Plasminogen activator inhibitor from human fibrosarcoma cells binds urokinase-type plasminogen activator, but not its proenzyme.
Husain et al. Purification and partial characterization of a single-chain high-molecular-weight form of urokinase from human urine
Wun et al. A proenzyme form of human urokinase.
Rijken et al. Fibrinolytic properties of one-chain and two-chain human extrinsic (tissue-type) plasminogen activator
Stump et al. Purification and characterization of single-chain urokinase-type plasminogen activator from human cell cultures.
Skriver et al. Plasminogen activator released as inactive proenzyme from murine cells transformed by sarcoma virus
Kasai et al. Proteolytic cleavage of single-chain pro-urokinase induces conformational change which follows activation of the zymogen and reduction of its high affinity for fibrin.
Stump et al. Purification and characterization of a novel low molecular weight form of single-chain urokinase-type plasminogen activator.
Gurewich et al. Inactivation of single-chain urokinase (pro-urokinase) by thrombin and thrombin-like enzymes: relevance of the findings to the interpretation of fibrin-binding experiments
Rijken et al. Isolation and functional characterization of the heavy and light chains of human tissue-type plasminogen activator.
Kohno et al. Kidney plasminogen activator: a precursor form of human urokinase with high fibrin affinity
De Munk et al. Acceleration of the thrombin inactivation of single chain urokinase-type plasminogen activator (pro-urokinase) by thrombomodulin.
Declerck et al. A monoclonal antibody specific for two-chain urokinase-type plasminogen activator. Application to the study of the mechanism of clot lysis with single-chain urokinase-type plasminogen activator in plasma
Binnema et al. The contact-system dependent plasminogen activator from human plasma: identification and characterization
Corti et al. Purification and characterization of single-chain urokinase-type plasminogen activator (pro-urokinase) from human A431 cells
Lijnen et al. Effect of fibrin-like stimulators on the activation of plasminogen by tissue-type plasminogen activator (t-PA)-studies with active site mutagenized plasminogen and plasmin resistant t-PA
Kohnert et al. A variant of tissue plasminogen activator (t-PA) comprised of the kringle 2 and the protease domain shows a significant difference in the in vitro rate of plasmin formation as compared to the recombinant human t-PA from transformed Chinese hamster ovary cells
Opdenakker et al. Influence of carbohydrate side chains on activity of tissue-type plasminogen activator
Strickland et al. Purification and properties of a plasminogen activator from cultured rat prostate adenocarcinoma cells
Mitsubayashi et al. Plasminogen activator in bladder tumors
Verheijen Purification, assay, and standardization of t-PA
Bando et al. Thrombolytic effect of pro-urokinase in vitro
EP0247674B1 (en) Plasminogen activator and thrombolytic composition