LILACS – Literatura Latinoamericana y del Caribe de Ciencias de la Salud

Relationship between antifungal susceptibility profile and virulence factors in Candida albicans isolated from nail specimens

Mohammadi, Faezeh; Ghasemi, Zeinab; Familsatarian, Behnaz; Salehi, Eelham; Sharifynia, Somayeh; Barikani, Ameneh; mirzadeh, Monirsadat; Hosseini, Mohammad Ali.

Rev. Soc. Bras. Med. Trop; 53 (), 2020

Abstract INTRODUCTION: The aim of this study was to evaluate some virulence factors in Candida albicans isolates from patients with onychomycosis and determine the correlation between these factors and the antifungal resistance profile. METHODS: Seventy species of C. albicans were confirmed using pol...

Antifúngicos/farmacología, Proteasas de Ácido Aspártico/biosíntesis, Biopelículas/crecimiento & desarrollo, Candida albicans/efectos de los fármacos, Candida albicans/patogenicidad, Candida albicans/ultraestructura, Farmacorresistencia Fúngica, Hemólisis, Pruebas de Sensibilidad Microbiana, Microscopía Electrónica de Rastreo, Uñas/microbiología, Onicomicosis/microbiología, Fosfolipasas/biosíntesis, Reacción en Cadena de la Polimerasa, Factores de Virulencia

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Purification and enzymatic characterization of a novel metalloprotease from Lachesis muta rhombeata snake venom

Cordeiro, Francielle Almeida; Coutinho, Bárbara Marques; Wiezel, Gisele Adriano; Bordon, Karla de Castro Figueiredo; Bregge-Silva, Cristiane; Rosa-Garzon, Nathalia Gonsales; Cabral, Hamilton; Ueberheide, Beatrix; Arantes, Eliane Candiani.

J. venom. anim. toxins incl. trop. dis; 24 (), 2018

Lachesis muta rhombeata (Lmr) is the largest venomous snake in Latin America and its venom contains mainly enzymatic components, such as serine and metalloproteases, L-amino acid oxidase and phospholipases A2. Metalloproteases comprise a large group of zinc-dependent proteases that cleave basement membra...

Venenos de Serpiente, Metaloproteasas, Lachesis muta, Proteasas de Ácido Aspártico, Péptido Hidrolasas

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Purification and characterization of an aspartic protease from the Rhizopus oryzae protease extract, Peptidase R

Hsiao, Nai-Wan; Chen, Yeh; Kuan, Yi-Chia; Lee, Yen-Chung; Lee, Shuo-Kang; Chan, Hsin-Hua; Kao, Chao-Hung.

Electron. j. biotechnol; 17 (2), 2014

Background Aspartic proteases are a subfamily of endopeptidases that are useful in a variety of applications, especially in the food processing industry. Here we describe a novel aspartic protease that was purified from Peptidase R, a commercial protease preparation derived from Rhizopus oryzae. Results ...

Proteasas de Ácido Aspártico/aislamiento & purificación, Rhizopus oryzae/química, Rhizopus oryzae/enzimología, Cromatografía, Industria de Alimentos, Endopeptidasas, Peso Molecular, Proteasas de Ácido Aspártico/metabolismo, Secuencia de Aminoácidos, Concentración de Iones de Hidrógeno, Temperatura

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