About: Pancreatic elastase

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An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

class of enzymes

Attributes	Values
rdf:type	Item
owl:sameAs	Pancreatic elastase
description	class of enzymes (en) enzima (it) enzyme (fr) клас ферментів (uk) Verdauungsenzym (de)
rdfs:label	Elastase pancreática (gl) Elastasi pancreatica (it) Pancreaselastase (nl) Pancreatic elastase (en) Pankreas-Elastase (de) Pankreasna elastaza (sr) Pankreasna elastaza (sh) Панкреатическая эластаза (ru)
skos:prefLabel	Elastase pancreática (gl) Elastasi pancreatica (it) Pancreaselastase (nl) Pancreatic elastase (en) Pankreas-Elastase (de) Pankreasna elastaza (sr) Pankreasna elastaza (sh) Панкреатическая эластаза (ru)
name	Elastase pancreática (gl) Elastasi pancreatica (it) Pancreaselastase (nl) Pancreatic elastase (en) Pankreas-Elastase (de) Pankreasna elastaza (sr) Pankreasna elastaza (sh) Панкреатическая эластаза (ru)
Freebase ID	wds:Q976747-0775B21F-E796-4B9E-A59F-F1D6057A4EC2
Freebase ID	/m/02p9hcl
instance of	wds:Q976747-774F7461-CE6F-46BC-9809-5B53FC500298
instance of	group or class of enzymes
subclass of	wds:Q976747-042f3509-4fd5-6aa3-18fc-e5c69fe476e5
subclass of	serine endopeptidase
molecular function	wds:Q976747-b6fc90ec-4f86-eef2-cf7e-ed45d6785df3
molecular function	serine-type endopeptidase activity
Commons category	wds:Q976747-53dccb14-580d-428b-90c9-7e781de2493c
Commons category	Pancreatic elastases
OpenAlex ID	wds:Q976747-9A0B955F-B0E4-4DBA-B75B-02C6E2A0891B
MeSH descriptor ID	wds:Q976747-4231C316-8609-4163-9133-5DE49255CE1A
Microsoft Academic ID	wds:Q976747-FA6E8F78-AD61-479C-A915-E87AA0885553
MeSH tree code	wds:Q976747-9fdaff1b-4026-d6e4-2df9-b760d2fa3805 wds:Q976747-c29013e2-4d46-4b08-08bd-a87f9587d014
MeSH descriptor ID	http://id.nlm.nih.gov/mesh/D010196
Microsoft Academic ID	https://makg.org/entity/2776326425
MeSH tree code	http://id.nlm.nih.gov/mesh/D08.811.277.656.300.760.560 http://id.nlm.nih.gov/mesh/D08.811.277.656.959.350.560
OpenAlex ID	C2776326425
MeSH descriptor ID	D010196
Microsoft Academic ID	2776326425
MeSH tree code	D08.811.277.656.300.760.560 D08.811.277.656.959.350.560
EC enzyme number	wds:Q976747-CA620399-A12A-41BA-8F96-19DF69A10E02
EC enzyme number	3.4.21.36
is about of	Pancreatic elastase https://www.wikidata.org/wiki/Special:EntityData/Q976747 Pancreatic elastase https://de.wikipedia.org/wiki/Pankreas-Elastase Category:Pancreatic elastases https://ru.wikipedia.org/wiki/%D0%9F%D0%B0%D0%BD%D0%BA%D1%80%D0%B5%D0%B0%D1%82%D0%B8%D1%87%D0%B5%D1%81%D0%BA%D0%B0%D1%8F_%D1%8D%D0%BB%D0%B0%D1%81%D1%82%D0%B0%D0%B7%D0%B0 https://it.wikipedia.org/wiki/Elastasi_pancreatica https://gl.wikipedia.org/wiki/Elastase_pancre%C3%A1tica https://nl.wikipedia.org/wiki/Pancreaselastase https://sh.wikipedia.org/wiki/Pankreasna_elastaza https://sr.wikipedia.org/wiki/Pankreasna_elastaza
is main subject of	Competitive labelling, a method for determining the reactivity of individual groups in proteins. The amino groups of porcine elastase Limited degradation of the third component (C3) of human complement by human leukocyte elastase (HLE): partial characterization of C3 fragments Crystal structure of elastase-substrate complex at -- 55 degrees C Isolation and Characterization of Porcine Proelastase The atomic structure of crystalline porcine pancreatic elastase at 2.5 Å resolution: Comparisons with the structure of α-chymotrypsin The active site of porcine elastase The primary structure of aspartate aminotransferase from pig heart muscle. Partial sequences determined by digestion with thermolysin and elastase Human Leucocyte Elastase and Cathepsin G: Structural and Functional Characteristics The induction of emphysema with elastase. II. Changes in connective tissue Tertiary structural differences between microbial serine proteases and pancreatic serine enzymes Action of Proteolytic Enzymes on Tropocollagen and Insoluble Collagen* Experimental emphysema induced with purified human neutrophil elastase: tissue localization of the instilled protease PRODUCTION OF ELASTASE AND PROTEINASE BY PSEUDOMONAS AERUGINOSA The folding of pancreatic elastase: independent domain refolding and inter-domain interaction Evolutionary Similarities between Pancreatic Proteolytic Enzymes PSEUDOMONAS AERUGINOSA ELASTASE. ISOLATION, CRYSTALLIZATION, AND PRELIMINARY CHARACTERIZATION A comparison of properties of the α-lytic protease of Sorangium sp. and porcine elastase Proteases from purulent sputum. Purification and properties of the elastase and chymotrypsin-like enzymes CHEMICAL COMPOSITION OF ENZYME-FRACTIONATED AGED HEART TISSUE Effects of Granulocyte Neutral Proteases on Complement Components Irreversible bronchial goblet cell metaplasia in hamsters with elastase-induced panacinar emphysema The induction of emphysema with elastase. I. The evolution of the lesion and the influence of serum CARDIOVASCULAR STUDIES ON COPPER-DEFICIENT SWINE. 8. ELASTIN CONTENT OF AORTA DETERMINED BY ELASTASE DIGESTION AND FORMIC ACID EXTRACTION Elastase-catalyzed amide hydrolysis of triand tetrapeptide amides Restrictions on the binding of proline-containing peptides to elastase Specificity of elastase. Hydrolysis of peptide p-nitrobenzyl esters Characterization of trypsin and elastase from the moose (Alces alces) I. Animo acid composition and specificity towards polypeptides Acetyl-L-alanyl-L-alanyl-L-alanine methyl ester: a new highly specific elastase substrate Microbial Elastases. A Comparative Study Impaired Enteric Degradation of Pancreatic Endopeptidases in Antibiotic-Treated Rats DETERMINATION OF ELASTASE AND ELASTASE INHIBITOR BY MEANS OF ORCEIN-ELASTIN Alkyl isocyanates as active-site-specific reagents for serine protease. Identification of the active-site serine as the site of reaction

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