Please use this identifier to cite or link to this item: https://biore.bio.bg.ac.rs/handle/123456789/7273
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dc.contributor.authorLavrenova, V. N.en_US
dc.contributor.authorKreyer, V. G.en_US
dc.contributor.authorSavković, Željkoen_US
dc.contributor.authorOsmolovskiy, A. A.en_US
dc.date.accessioned2024-09-06T10:39:45Z-
dc.date.available2024-09-06T10:39:45Z-
dc.date.issued2024-02-01-
dc.identifier.issn00036838-
dc.identifier.urihttps://biore.bio.bg.ac.rs/handle/123456789/7273-
dc.description.abstractThe extracellular protease with protein C-like and plasmin-like activities was isolated from the culture fluid of the micromycete A. tabacinus BEOFB3260m. It has been established that A. tabacinus extracellular protease is a non-glycosylated serine protease with molecular weight about 30 kDa. The enzyme is active and stable at 25–37°C, active at pH 7.0–12.0 and stable at pH 3.0–12.0 and is a promising candidate for the development of new anticoagulant drugs.en_US
dc.publisherM A I K Nauka - Interperiodicaen_US
dc.relation.ispartofApplied Biochemistry and Microbiologyen_US
dc.subjectanticoagulantsen_US
dc.subjectAspergillus tabacinusen_US
dc.subjectchromogenic peptide substratesen_US
dc.subjectfibrinolytic enzymesen_US
dc.subjectproteasesen_US
dc.titleProperties of Extracellular Protease—Regulator of Hemostasis Produced by Micromycete Aspergillus tabacinusen_US
dc.typeArticleen_US
dc.identifier.doi10.1134/S0003683824010101-
dc.identifier.scopus2-s2.0-85189078039-
dc.identifier.urlhttps://api.elsevier.com/content/abstract/scopus_id/85189078039-
dc.description.rankM23en_US
dc.description.impact1.0en_US
dc.description.startpage118en_US
dc.description.endpage123en_US
dc.relation.issn0003-6838en_US
dc.description.volume60en_US
dc.description.issue1en_US
item.fulltextNo Fulltext-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.grantfulltextnone-
item.openairetypeArticle-
item.cerifentitytypePublications-
crisitem.author.deptChair of Algology, Mycology and Lichenology-
crisitem.author.orcid0000-0002-6678-4958-
Appears in Collections:Journal Article
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