Matches in SemOpenAlex for { <https://semopenalex.org/work/W1920092488> ?p ?o ?g. }
Showing items 1 to 99 of
99
with 100 items per page.
- W1920092488 endingPage "2157" @default.
- W1920092488 startingPage "2149" @default.
- W1920092488 abstract "Extracellular proteases have been suggested to be virulence factors in invasive aspergillosis. Since serine protease gene-disrupted mutants retain virulence, other proteases are suspected to be also involved in the degradation of lung structural material. An elastinolytic neutral metalloprotease was purified 320-fold from the extracellular fluid of Aspergillus fumigatus grown on elastin by affinity chromatography on bacitracin-Sepharose 4B and gel filtration on Sephadex G-75. The molecular mass was determined to be 43 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. No carbohydrate was attached to this metalloprotease, and its first 22 N-terminal amino acids did not show any homology with the known metalloproteases. The enzyme was completely inhibited by EDTA, 1,10-phenanthroline, and phosphoramidon but not by inhibitors specific for serine, aspartate, and cysteine proteases. Zn2+ and, to a lesser extent, Co2+ reversed the inhibition caused by 1,10-phenanthroline. The protease hydrolyzed the peptide bonds His-Leu, Ala-Leu, Tyr-Leu, Gly-Phe, and Phe-Phe in the B chain of insulin. Synthetic substrate Abz-Ala-Ala-Phe-Phe-pNA could be used for the fluorimetric assay of the A. fumigatus metalloprotease. This enzyme had maximum activity in the pH range 7.5 to 8.0 and at 60 degrees C. It retained 50% of the protease activity when held at 60 degrees C for 1 h. Zn2+ and Co2+ at 1 mM did not inhibit the protease activity. The metalloprotease was able to hydrolyze elastin, and its elastinolytic activity was comparable to that of the serine protease from this organism. The presence of Zn2+ in the culture medium stimulated the metalloprotease production. Rabbit antibodies prepared against the enzyme severely inhibited the enzyme activity. Immunogold electron microscopy revealed that A. fumigatus invading neutropenic mouse lungs secretes this metalloprotease." @default.
- W1920092488 created "2016-06-24" @default.
- W1920092488 creator A5009189005 @default.
- W1920092488 creator A5011765239 @default.
- W1920092488 creator A5018542352 @default.
- W1920092488 creator A5087857077 @default.
- W1920092488 date "1994-06-01" @default.
- W1920092488 modified "2023-10-13" @default.
- W1920092488 title "Purification and characterization of an elastinolytic metalloprotease from Aspergillus fumigatus and immunoelectron microscopic evidence of secretion of this enzyme by the fungus invading the murine lung" @default.
- W1920092488 cites W1491021866 @default.
- W1920092488 cites W1722214742 @default.
- W1920092488 cites W1804076655 @default.
- W1920092488 cites W1831668674 @default.
- W1920092488 cites W1889896208 @default.
- W1920092488 cites W1932052686 @default.
- W1920092488 cites W1935518068 @default.
- W1920092488 cites W1960821628 @default.
- W1920092488 cites W2039493936 @default.
- W1920092488 cites W2048083566 @default.
- W1920092488 cites W2051251601 @default.
- W1920092488 cites W2067805144 @default.
- W1920092488 cites W2100837269 @default.
- W1920092488 cites W2101108802 @default.
- W1920092488 cites W2124814621 @default.
- W1920092488 cites W2144526814 @default.
- W1920092488 cites W2152337140 @default.
- W1920092488 cites W2157885858 @default.
- W1920092488 cites W2161686892 @default.
- W1920092488 cites W4231850718 @default.
- W1920092488 cites W4252293012 @default.
- W1920092488 cites W4293247451 @default.
- W1920092488 doi "https://doi.org/10.1128/iai.62.6.2149-2157.1994" @default.
- W1920092488 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/186491" @default.
- W1920092488 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8188335" @default.
- W1920092488 hasPublicationYear "1994" @default.
- W1920092488 type Work @default.
- W1920092488 sameAs 1920092488 @default.
- W1920092488 citedByCount "146" @default.
- W1920092488 countsByYear W19200924882012 @default.
- W1920092488 countsByYear W19200924882013 @default.
- W1920092488 countsByYear W19200924882014 @default.
- W1920092488 countsByYear W19200924882015 @default.
- W1920092488 countsByYear W19200924882016 @default.
- W1920092488 countsByYear W19200924882017 @default.
- W1920092488 countsByYear W19200924882018 @default.
- W1920092488 countsByYear W19200924882019 @default.
- W1920092488 countsByYear W19200924882020 @default.
- W1920092488 countsByYear W19200924882021 @default.
- W1920092488 countsByYear W19200924882022 @default.
- W1920092488 countsByYear W19200924882023 @default.
- W1920092488 crossrefType "journal-article" @default.
- W1920092488 hasAuthorship W1920092488A5009189005 @default.
- W1920092488 hasAuthorship W1920092488A5011765239 @default.
- W1920092488 hasAuthorship W1920092488A5018542352 @default.
- W1920092488 hasAuthorship W1920092488A5087857077 @default.
- W1920092488 hasBestOaLocation W19200924881 @default.
- W1920092488 hasConcept C153911025 @default.
- W1920092488 hasConcept C181199279 @default.
- W1920092488 hasConcept C182220744 @default.
- W1920092488 hasConcept C2776714187 @default.
- W1920092488 hasConcept C2777807008 @default.
- W1920092488 hasConcept C2779787849 @default.
- W1920092488 hasConcept C55493867 @default.
- W1920092488 hasConcept C55728118 @default.
- W1920092488 hasConcept C86803240 @default.
- W1920092488 hasConcept C89423630 @default.
- W1920092488 hasConceptScore W1920092488C153911025 @default.
- W1920092488 hasConceptScore W1920092488C181199279 @default.
- W1920092488 hasConceptScore W1920092488C182220744 @default.
- W1920092488 hasConceptScore W1920092488C2776714187 @default.
- W1920092488 hasConceptScore W1920092488C2777807008 @default.
- W1920092488 hasConceptScore W1920092488C2779787849 @default.
- W1920092488 hasConceptScore W1920092488C55493867 @default.
- W1920092488 hasConceptScore W1920092488C55728118 @default.
- W1920092488 hasConceptScore W1920092488C86803240 @default.
- W1920092488 hasConceptScore W1920092488C89423630 @default.
- W1920092488 hasIssue "6" @default.
- W1920092488 hasLocation W19200924881 @default.
- W1920092488 hasLocation W19200924882 @default.
- W1920092488 hasLocation W19200924883 @default.
- W1920092488 hasOpenAccess W1920092488 @default.
- W1920092488 hasPrimaryLocation W19200924881 @default.
- W1920092488 hasRelatedWork W124183450 @default.
- W1920092488 hasRelatedWork W1596676072 @default.
- W1920092488 hasRelatedWork W2068975409 @default.
- W1920092488 hasRelatedWork W2109018839 @default.
- W1920092488 hasRelatedWork W2124956779 @default.
- W1920092488 hasRelatedWork W2153970031 @default.
- W1920092488 hasRelatedWork W2159000061 @default.
- W1920092488 hasRelatedWork W2182122486 @default.
- W1920092488 hasRelatedWork W3195890830 @default.
- W1920092488 hasRelatedWork W3207552102 @default.
- W1920092488 hasVolume "62" @default.
- W1920092488 isParatext "false" @default.
- W1920092488 isRetracted "false" @default.
- W1920092488 magId "1920092488" @default.
- W1920092488 workType "article" @default.