Barszcz et al., 1988 - Google Patents

Alpha1-proteinase inhibitor in psoriasis: reduced activity in symptom-free patients and during flare

Barszcz et al., 1988

Document ID: 17297804106707954338
Author: Barszcz D; Zarębska Z; Glińska-Ferenz M; Jablońska S; Tigalonowa M; Gliński W
Publication year: 1988
Publication venue: Archives of dermatological research

External Links

Cited by

Snippet

The aim of this study was to quantitate the active fraction of the α1-proteinase inhibitor (α1- PI) in psoriasis. Serum proteinase inhibitory capacity was measured vs porcine pancreatic elastase of a known active fraction against its specific substrate (Suc-Ala3-pNA). The …

Continue reading at link.springer.com (other versions)

201000004681 psoriasis 0 title abstract description 71

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
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/55—Protease inhibitors
- A61K38/57—Protease inhibitors from animals; from humans
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/81—Protease inhibitors
- C07K14/8107—Endopeptidase (E.C. 3.4.21-99) inhibitors
- C07K14/811—Serine protease (E.C. 3.4.21) inhibitors
- 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)
- 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
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/43—Enzymes; Proenzymes; Derivatives thereof

Similar Documents

Publication	Publication Date	Title
KAFIENAH et al.	1998	Cleavage of native type I collagen by human neutrophil elastase
Olson et al.	2002	Heparin activates antithrombin anticoagulant function by generating new interaction sites (exosites) for blood clotting proteinases
Desrochers et al.	1991	Interstitial collagenase (matrix metalloproteinase-1) expresses serpinase activity.
Weiss et al.	1986	Collagenolytic metalloenzymes of the human neutrophil: characteristics, regulation and potential function in vivo
Kruithof	1988	Plasminogen activator inhibitors-a review
Janoff	1972	Human granulocyte elastase. Further delineation of its role in connective tissue damage
Horrevoets	2004	review Plasminogen activator inhibitor 1 (PAI-1): in vitro activities and clinical relevance.
Yarovaya et al.	2002	Contact system. New concepts on activation mechanisms and bioregulatory functions
DIETL et al.	1979	Human inter-α-trypsin inhibitor. Limited proteolysis by trypsin, plasmin, kallikrein and granulocytic elastase and inhibitory properties of the cleavage products
Wang et al.	1985	Latent and active plasminogen activator in corneal ulceration.
EP0724600B1 (en)	2002-02-13	Process for preparing an inter-alpha-trypsine inhibitor concentrate for therapeutical use, and concentrate thus obtained
Guyot et al.	2005	Proteolytic susceptibility of the serine protease inhibitor trappin-2 (pre-elafin): evidence for tryptase-mediated generation of elafin
Vogelmeier et al.	1997	Comparative loss of activity of recombinant secretory leukoprotease inhibitor and alpha 1-protease inhibitor caused by different forms of oxidative stress
Clemmensen	1978	Inhibition of urokinase by complex formation with human antithrombin III in absence and presence of heparin
Scott et al.	1982	Effect of heparin on the inactivation rate of human factor XIa by antithrombin-III
Takahara et al.	1983	Inhibitory spectrum of mouse contrapsin and α-1-antitrypsin against mouse serine proteases
Barszcz et al.	1988	Alpha1-proteinase inhibitor in psoriasis: reduced activity in symptom-free patients and during flare
Carbini et al.	1993	The molecular biology of the kallikrein–kinin system: III. The human kallikrein gene family and kallikrein substrate
Sherman et al.	1995	Identification of tissue-type plasminogen activator-specific plasminogen activator inhibitor-1 mutants: evidence that second sites of interaction contribute to target specificity
EP0398859B1 (en)	1994-11-30	Novel 92-kDa type IV collagenase
Lim et al.	1996	Independent regulation of matrix metalloproteinases and plasminogen activators in human fibrosarcoma cells
Tsushima et al.	1991	Characterization of a cathepsin‐H‐like enzyme from a human melanoma cell line
Redini et al.	1988	Influence of heparin fragments on the biological activities of elastase (s) and α1 proteinase inhibitor
Ciaccia et al.	1997	Heparin promotes proteolytic inactivation by thrombin of a reactive site mutant (L444R) of recombinant heparin cofactor II
Cooper et al.	1995	Reactive site mutants of recombinant protein C inhibitor