FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2052036575> ?p ?o ?g. }

• W2052036575 abstract "Abstract Elastinolytic protease in human blood platelets Experiments are described devised in order to study the of elastinolytic protease(s) from human blood platelet suspensions as well as the separation of these proteases from the acid-cathepsins, their partial purification and characterization. ADP, adrenaline, and collagen produced a significant of the elastinolytic activity of the platelet suspension as well as a partial of this activity in the supernatant. Triton-X-100 and sonication produced a strong and a near 100% liberation of the elastinolytic activity. This suggested the existence of two different and independent mechanisms: activation and liberation. Triton-X-100 stabilised the elastinolytic activity sufficiently to render possible its partial purification. Ammonium sulfate at 40% saturation precipitated most of the acid-catheptic activity. This activity could be further purified by gel-filtration on Sephadex G 200. The partially purified acid-cathepsin fraction was not activated by mercaptoethanol and migrated with the mobility of γ-globulins. Its behaviour reminds that of the cathepsin C isolated from carrageenine granuloma extracts 8,9 . About half of the elastinolytic activity remained in the 60% ammonium sulfate supernatant and was not further purified. Part of it (approx. 8%) precipitated at 60% ammonium sulfate and was further separated on Sephadex G-200 in two peaks; the first, excluded peak (approx. 90% of total proteins charged) having a specific activity of 21,400 counts/min/mg protein; the second, penetrating the column (approx. 5% of total protein, ⋍ 1.2 mg) having a specific activity of 144,000 counts/min/mg protein. The first fraction was still heterogenous, with a major band migrating with the albumins. Its pH optimum is near 8.0, it is strongly inhibited by Ca 2+ which precipitates it. The other agents of platelet aggregation (ADP, adrenaline, EDTA, 5-hydroxytryptamine) had only a weak activating or inhibiting action. These experiments confirm the presence of several proteolytic enzymes in human blood platelet preparations and show that the elastolytic protease is distinct from the major acid-catheptic enzymes. The elastolytic enzymes may be present in several protein fractions or they may have several forms differing in molecular weight. Further experiments should clarify this point." @default.
• W2052036575 created "2016-06-24" @default.
• W2052036575 creator A5006467698 @default.
• W2052036575 creator A5028119214 @default.
• W2052036575 creator A5036030299 @default.
• W2052036575 creator A5042278227 @default.
• W2052036575 creator A5079730878 @default.
• W2052036575 creator A5006327886 @default.
• W2052036575 date "1970-11-01" @default.
• W2052036575 modified "2023-10-14" @default.
• W2052036575 title "Études sur une protéase élastinolytique des plaquettes sanguines humaines" @default.
• W2052036575 cites W1554243268 @default.
• W2052036575 cites W1554921443 @default.
• W2052036575 cites W1775749144 @default.
• W2052036575 cites W1977994076 @default.
• W2052036575 cites W2012388970 @default.
• W2052036575 cites W2028581450 @default.
• W2052036575 cites W2030461289 @default.
• W2052036575 cites W2033675758 @default.
• W2052036575 cites W2040568655 @default.
• W2052036575 cites W2041434161 @default.
• W2052036575 cites W2058798515 @default.
• W2052036575 cites W2072860427 @default.
• W2052036575 cites W2092246546 @default.
• W2052036575 cites W2094399124 @default.
• W2052036575 cites W2114329602 @default.
• W2052036575 cites W2292192524 @default.
• W2052036575 doi "https://doi.org/10.1016/0021-9150(70)90049-3" @default.
• W2052036575 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/5503381" @default.
• W2052036575 hasPublicationYear "1970" @default.
• W2052036575 type Work @default.
• W2052036575 sameAs 2052036575 @default.
• W2052036575 citedByCount "8" @default.
• W2052036575 countsByYear W20520365752017 @default.
• W2052036575 crossrefType "journal-article" @default.
• W2052036575 hasAuthorship W2052036575A5006327886 @default.
• W2052036575 hasAuthorship W2052036575A5006467698 @default.
• W2052036575 hasAuthorship W2052036575A5028119214 @default.
• W2052036575 hasAuthorship W2052036575A5036030299 @default.
• W2052036575 hasAuthorship W2052036575A5042278227 @default.
• W2052036575 hasAuthorship W2052036575A5079730878 @default.
• W2052036575 hasConcept C163994747 @default.
• W2052036575 hasConcept C167844969 @default.
• W2052036575 hasConcept C181199279 @default.
• W2052036575 hasConcept C185592680 @default.
• W2052036575 hasConcept C193363816 @default.
• W2052036575 hasConcept C198684833 @default.
• W2052036575 hasConcept C2776714187 @default.
• W2052036575 hasConcept C2780925461 @default.
• W2052036575 hasConcept C43617362 @default.
• W2052036575 hasConcept C55493867 @default.
• W2052036575 hasConceptScore W2052036575C163994747 @default.
• W2052036575 hasConceptScore W2052036575C167844969 @default.
• W2052036575 hasConceptScore W2052036575C181199279 @default.
• W2052036575 hasConceptScore W2052036575C185592680 @default.
• W2052036575 hasConceptScore W2052036575C193363816 @default.
• W2052036575 hasConceptScore W2052036575C198684833 @default.
• W2052036575 hasConceptScore W2052036575C2776714187 @default.
• W2052036575 hasConceptScore W2052036575C2780925461 @default.
• W2052036575 hasConceptScore W2052036575C43617362 @default.
• W2052036575 hasConceptScore W2052036575C55493867 @default.
• W2052036575 hasLocation W20520365751 @default.
• W2052036575 hasLocation W20520365752 @default.
• W2052036575 hasOpenAccess W2052036575 @default.
• W2052036575 hasPrimaryLocation W20520365751 @default.
• W2052036575 hasRelatedWork W1994711691 @default.
• W2052036575 hasRelatedWork W2011881892 @default.
• W2052036575 hasRelatedWork W2162625483 @default.
• W2052036575 hasRelatedWork W2341920515 @default.
• W2052036575 hasRelatedWork W2346048935 @default.
• W2052036575 hasRelatedWork W2359219901 @default.
• W2052036575 hasRelatedWork W2748952813 @default.
• W2052036575 hasRelatedWork W2899084033 @default.
• W2052036575 hasRelatedWork W2950036879 @default.
• W2052036575 hasRelatedWork W3136415254 @default.
• W2052036575 isParatext "false" @default.
• W2052036575 isRetracted "false" @default.
• W2052036575 magId "2052036575" @default.
• W2052036575 workType "article" @default.