Please use this identifier to cite or link to this item: https://biore.bio.bg.ac.rs/handle/123456789/482
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dc.contributor.authorStamenković Radak, Marinaen_US
dc.contributor.authorMilanovic, Mirjanaen_US
dc.contributor.authorSavic, Tatjanaen_US
dc.contributor.authorAndjelkovic, Markoen_US
dc.date.accessioned2019-07-03T13:09:31Z-
dc.date.available2019-07-03T13:09:31Z-
dc.date.issued2003-01-01-
dc.identifier.issn1341-7568-
dc.identifier.urihttps://biore.bio.bg.ac.rs/handle/123456789/482-
dc.description.abstractBiochemical properties of enzyme α-amylase were surveyed in Drosophila obscura Old world group of species (D. subobscura, D. ambigua, D. obscura and D. tristis) sampled in the same habitat, with the aim to reveal some ecological and evolutionary aspects of amylase polymorphism, which has been studied extensively in D. subobscura, but not compared with other species in the group. The data obtained show that D. subobscura is distinct from the other three species regarding all biochemical amylase properties. Such a divergence also correlates with the niche breadth and relative abundance of these species in the same habitat.en_US
dc.language.isoenen_US
dc.relation.ispartofGenes and Genetic Systemsen_US
dc.subjectAmylaseen_US
dc.subjectDrosophila ecologyen_US
dc.subjectEnzyme activityen_US
dc.subjectObscura speciesen_US
dc.titleAdaptive significance of amylase polymorphism in Drosophila XIII. Old world obscura species subgroup divergence according to biochemical properties of α-amylaseen_US
dc.typeArticleen_US
dc.identifier.doi10.1266/ggs.78.23-
dc.identifier.pmid12655135-
dc.identifier.scopus2-s2.0-0037303065-
dc.identifier.urlhttps://api.elsevier.com/content/abstract/scopus_id/0037303065-
item.languageiso639-1en-
item.cerifentitytypePublications-
item.openairetypeArticle-
item.fulltextNo Fulltext-
item.grantfulltextnone-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
crisitem.author.deptChair of Genetics and Evolution-
crisitem.author.orcid0000-0002-6937-7282-
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