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Substrate specificity of membrane-bound alcohol oxidase from the tobacco hornworm moth (Manduca sexta) female pheromone glands

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F06%3A00038947" target="_blank" >RIV/61388963:_____/06:00038947 - isvavai.cz</a>

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    Substrate specificity of membrane-bound alcohol oxidase from the tobacco hornworm moth (Manduca sexta) female pheromone glands

  • Original language description

    A putative alcohol oxidase (AO) from abdominal tips (ATs) of Manduca sexta virgin females was studied in a biphasic system hexane/aqueous phosphate buffer. The pH optimum closest to neutral range (6.8) and the temperature optimum closest to room temperature (25+/-3 C) were measured for the highest AO activity. A high selectivity for primary alcohols of benzylic, saturated, and allylic type was observed.

  • Czech name

    Substrátová specifita membránové alkohol-oxidasy z feromonálních žláz samic lišaje tabákového

  • Czech description

    Alkohol-oxidasa z feromonálních žláz samic lišaje tabákového byla studována v systému hexan/fosfátový pufr. Bylo nalezeno pH optimum 6,8 a optimální teplota 25+/-3 C pro maximální enzymovou aktivitu. Byla nalezena vysoká selektivita pro primární alkoholyjak nasycené, tak benzylového či allylového typu.

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CC - Organic chemistry

  • OECD FORD branch

Result continuities

  • Project

  • Continuities

    Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2006

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Journal of Molecular Catalysis B-Enzymatic

  • ISSN

    1381-1177

  • e-ISSN

  • Volume of the periodical

    38

  • Issue of the periodical within the volume

    1

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    6

  • Pages from-to

    37-42

  • UT code for WoS article

  • EID of the result in the Scopus database