elastase


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elastase

 [e-las´tās]
an enzyme capable of catalyzing the digestion of elastic tissue.

e·las·tase

(ē-las'tās),
A serine proteinase hydrolyzing elastin; other elastase-like enzymes have been identified, for example, pancreatic elastase (pancreatopeptidase E) and leukocyte elastase (lysosomal or neutrophil elastase), with different sequences and kinetic parameters; all have fairly broad specificities.

elastase

/elas·tase/ (e-las´tās) see pancreatic elastase.

elastase

(ĭ-lăs′tās, -tāz)
n.
Any of a class of enzymes that catalyze the hydrolysis of elastin, especially one that is found in pancreatic juice.

elastase

an enzyme that cleaves bonds adjacent to neutral amino acids in elastin.

elastase

(1) Pancreatic elastase, EC 3.4.21.11. 
(2) Leukocyte elastase, EC 3.4.21.37.

e·las·tase

(ĕ-las'tās)
A serine proteinase hydrolyzing elastin.

elastase

an enzyme capable of catalyzing the digestion of elastic tissue.
References in periodicals archive ?
Activated or necrotic neutrophils liberate human neutrophil elastase (hNE) in the lung that causes damage to structural, cellular and soluble components of the pulmonary microenvironment.
Table-1: DPPH radical scavenging effects and neutrophil elastase inhibiting effects of the crude extract fractions and isolates (1-10).
The inhibitory activity was determined by the difference between activity of the bacterial elastase without inhibitor and the residual activity of the same solution after adding the inhibitor.
Neutrophil elastase release was determined using SAAVNA as a substrate, and p-nitrophenol was measured spectrophotometrically according to modified assay of Liou et al.
Effects of ulinastatin on granulocyte elastase and fibronectin in patients undergoing cardiopulmonary bypass.
When the activities of protease (trypsinlike, chymotrypsin-like and elastase like) were compared at different pH, no significant differences were found; however, trypsin-like proteases shown the higher activity.
However, the sorption of proteins where Vm is the column dead volume (mL); such as cytochrome c, lysozyme, [beta]-lactoglobulin, elastase, albumin, and L-glutamic dehydrogenase was affected by the sorbent when acetonitrile was used as the mobile phase organic solvent.
In vitro tests, ulinastatin is reported to inhibit the production of TNF-[alpha] and IL-1 in Lipopolysaccharides (LPS)-stimulated human monocytes and HL60 cells or bronchial epithelial cells which were stimulated by LPS or neutrophil elastase.
The release of elastase from neutrophil lysosymes is believed to be mainly responsible for elastin degradation, ultimately resulting in the development of pathological processes in PE.
Elastase enzymatic degradation was performed as per the method described by Leach et al.