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  1. Article ; Online: Bothrops snake venom L-amino acid oxidases impair biofilm formation of clinically relevant bacteria.

    Alves de Melo Fernandes, Thales / Rafaella Costa, Tássia / de Paula Menezes, Ralciane / Arantes de Souza, Meliza / Gomes Martins, Carlos Henrique / Junior, Nilson Nicolau / Gobbi Amorim, Fernanda / Quinton, Loïc / Polloni, Lorena / Teixeira, Samuel Cota / Amália Vieira Ferro, Eloisa / Soares, Andreimar Martins / de Melo Rodrigues Ávila, Veridiana

    Toxicon : official journal of the International Society on Toxinology

    2023  Volume 238, Page(s) 107569

    Abstract: The present work addressed the abilities of two L-amino acid oxidases isolated from Bothrops moojeni (BmooLAAO-I) and Bothrops jararacussu (BjussuLAAO-II) snake venoms to control the growth and prevent the biofilm formation of clinically relevant ... ...

    Abstract The present work addressed the abilities of two L-amino acid oxidases isolated from Bothrops moojeni (BmooLAAO-I) and Bothrops jararacussu (BjussuLAAO-II) snake venoms to control the growth and prevent the biofilm formation of clinically relevant bacterial pathogens. Upon S. aureus (ATCC BAA44) and S. aureus (clinical isolates), BmooLAAO-I (MIC = 0.12 and 0.24 μg/mL, respectively) and BjussuLAAO-II (MIC = 0.15 μg/mL) showed a potent bacteriostatic effect. Against E. coli (ATCC BAA198) and E. coli (clinical isolates), BmooLAAO-I (MIC = 15.6 and 62.5 μg/mL, respectively) and BjussuLAAO-II (MIC = 4.88 and 9.76 μg/mL, respectively) presented a lower extent effect. Also, BmooLAAO-I (MICB
    MeSH term(s) Animals ; Crotalid Venoms/toxicity ; L-Amino Acid Oxidase/pharmacology ; L-Amino Acid Oxidase/chemistry ; Staphylococcus aureus ; Escherichia coli ; Bothrops ; Snake Venoms/chemistry ; Bacteria ; Biofilms ; Venomous Snakes
    Chemical Substances Crotalid Venoms ; L-Amino Acid Oxidase (EC 1.4.3.2) ; Snake Venoms
    Language English
    Publishing date 2023-12-19
    Publishing country England
    Document type Journal Article
    ZDB-ID 204479-1
    ISSN 1879-3150 ; 0041-0101
    ISSN (online) 1879-3150
    ISSN 0041-0101
    DOI 10.1016/j.toxicon.2023.107569
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 501: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  2. Article ; Online: Biochemical characterization and assessment of leishmanicidal effects of a new L-amino acid oxidase from Crotalus durissus collilineatus snake venom (CollinLA AO-I).

    de Freitas, Vitor / Costa, Tássia Rafaella / Nogueira, Amanda Rodrigues / Polloni, Lorena / Alves de Melo Fernandes, Thales / Correia, Lucas Ian Veloso / Borges, Bruna Cristina / Teixeira, Samuel Cota / Silva, Marcelo José Barbosa / Amorim, Fernanda Gobbi / Quinton, Loïc / Saraiva, André Lopes / Espindola, Foued Salmen / Iwai, Leo Kei / Rodrigues, Renata Santos / Yoneyama, Kelly Aparecida Geraldo / de Melo Rodrigues Ávila, Veridiana

    Toxicon : official journal of the International Society on Toxinology

    2023  Volume 230, Page(s) 107156

    Abstract: This study reports the isolation of CollinLAAO-I, a new L-amino acid oxidase from Crotalus durissus collilineatus snake venom, its biochemical characterization and leishmanicidal potential in Leishmania spp. CollinLAAO-I (63.1 kDa) was successfully ... ...

    Abstract This study reports the isolation of CollinLAAO-I, a new L-amino acid oxidase from Crotalus durissus collilineatus snake venom, its biochemical characterization and leishmanicidal potential in Leishmania spp. CollinLAAO-I (63.1 kDa) was successfully isolated with high purity using two chromatographic steps and represents 2.5% of total venom proteins. CollinLAAO-I displayed high enzymatic activity (4262.83 U/mg/min), significantly reducing after 28 days. The enzymatic activity of CollinLAAO-I revealed higher affinity for hydrophobic amino acids such as L-leucine, high enzymatic activity in a wide pH range (6.0-10.0), at temperatures from 0 to 25 °C, and showed complete inhibition in the presence of Na
    MeSH term(s) Animals ; L-Amino Acid Oxidase/chemistry ; Crotalid Venoms/chemistry ; Crotalus ; Snake Venoms
    Chemical Substances L-Amino Acid Oxidase (EC 1.4.3.2) ; Crotalid Venoms ; Snake Venoms
    Language English
    Publishing date 2023-05-09
    Publishing country England
    Document type Journal Article
    ZDB-ID 204479-1
    ISSN 1879-3150 ; 0041-0101
    ISSN (online) 1879-3150
    ISSN 0041-0101
    DOI 10.1016/j.toxicon.2023.107156
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 501: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

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