Results 31 to 40 of about 1,809,550 (296)

Thermostable α-galactosidase fromBacillus stearothermophilusNUB3621: cloning, sequencing and characterization [PDF]

FEMS Microbiology Letters, 1999
An alpha-galactosidase gene from the thermophilic bacterium Bacillus stearothermophilus NUB3621 was cloned, sequenced, expressed in Escherichia coli and the recombinant protein was purified. The Bacillus enzyme, designated AgaN, is similar to alpha-galactosidases of family 36 in the classification of glycosyl hydrolases.
O, Fridjonsson, H, Watzlawick, A, Gehweiler, R, Mattes   +3 more
openaire   +2 more sources

α‐Galactosidase‐A Loaded‐Nanoliposomes with Enhanced Enzymatic Activity and Intracellular Penetration [PDF]

Advanced Healthcare Materials, 2016
Lysosomal storage disorders (LSD) are caused by lysosomal dysfunction usually as a consequence of deficiency of a single enzyme required for the metabolism of macromolecules, such as lipids, glycoproteins, and mucopolysaccharides.
Ingrid Cabrera, I. Abasolo, J. Corchero, E. Elizondo, P. Gil, Evelyn Moreno, J. Faraudo, S. Sala, D. Bueno, E. González-Mira, Merche Rivas, Marta Melgarejo, Daniel Pulido, F. Albericio, M. Royo, A. Villaverde, M. Garcia-Parajo, S. Schwartz, N. Ventosa, J. Veciana   +19 more
semanticscholar   +2 more sources

Stability of native and modified α-galactosidase of Cladosporium cladosporioides [PDF]

The Ukrainian Biochemical Journal, 2015
By modifying carbohydrate component of glycoproteins it is possible to elucidate its role in manifestation of structural and functional properties of the enzyme. The comparison of activity and stability of the native and modified by oxidation with sodium
N. V. Borzova, L. D. Varbanets
doaj   +1 more source

The validation of pharmacogenetics for the identification of Fabry patients to be treated with migalastat [PDF]

, 2017
PURPOSE: Fabry disease is an X-linked lysosomal storage disorder caused by mutations in the α-galactosidase A gene. Migalastat, a pharmacological chaperone, binds to specific mutant forms of α-galactosidase A to restore lysosomal activity.
A Gal, AK Topaloglu, Benjamin Bronfin, C Filoni, Carrolee Barlow, CM Eng, Daniel G. Bichet, David J. Lockhart, Derralynn Hughes, Dominique P. Germain, DP Germain, DP Germain, DP Germain, DP Germain, E Conzelmann, Elfrida R. Benjamin, ER Benjamin, Evan Katz, Farhana Pruthi, FK Johnson, G Altarescu, GH Yam, GH Yam, Hadis Williams, J Lukas, J Shabbeer, Jay Barth, Jeff Castelli, John Kirk, JQ Fan, Julie Yu, Kenneth J. Valenzano, L Barisoni, L Echevarria, M Ries, Maria Cecilia Della Valle, MJ van Breemen, P Lemansky, R Giugliani, R Khanna, Raphael Schiffmann, RJ Desnick, RJ Desnick, RO Brady, Robert J. Desnick, Roberto Giugliani, S Ishii, Sarah Bond, SH Shin, SM Rombach, William R. Wilcox, WR Wilcox, X Wu, Xiaoyang Wu   +53 more
core   +1 more source

Dysregulated DNA methylation in the pathogenesis of Fabry disease

Molecular Genetics and Metabolism Reports, 2022
Fabry disease is an X-linked lysosomal storage disorder caused by a deficiency of α-galactosidase A and subsequent accumulation of glycosphingolipids with terminal α-D-galactosyl residues.
Jin-Song Shen, Uthra Balaji, Kunitoshi Shigeyasu, Yoshinaga Okugawa, Siamak Jabbarzadeh-Tabrizi, Taniqua S. Day, Erland Arning, John Marshall, Seng H. Cheng, Jinghua Gu, Raphael Schiffmann, Teodoro Bottiglieri, Ajay Goel   +12 more
doaj   +1 more source

Expression of β-galactosidase inRhizobium japonicum [PDF]

FEMS Microbiology Letters, 1985
The plasmid pGC91.14 was used to introduce via conjugation the Escherichia coli lac operon into fast-growing and slow-growing strains of Rhizobium japonicum. Exconjugants now expressed higher levels of β-galactosidase activity which was still inducible by isopropyl-β-d-thiogalactoside (IPTG).
openaire   +1 more source

Transcriptional analysis of the β-galactosidase gene (pbg) inClostridium perfringens [PDF]

FEMS Microbiology Letters, 1995
The mode of expression of the beta-galactosidase gene (pbg) of Clostridium perfringens was examined. The pbg gene was transcribed on a single 3.7-kb mRNA. The transcript contained a message for ORF54, located upstream of the pbg gene in the chromosome, indicating that ORF54 and the pbg gene comprise one operon (pbg operon). Expression of the pbg operon
T, Kobayashi, T, Shimizu, H, Hayashi
openaire   +2 more sources

Discovery of a Potent α ‑ Galactosidase Inhibitor by in Situ Analysis of a Library of Pyrrolizidine − (Thio)urea Hybrid Molecules Generated via Click Chemistry [PDF]

, 2018
The parallel synthesis of a 26-membered-library of aromatic/aliphatic-(thio)urea-linked pyrrolizidines followed by in situ biological evaluation toward α -galactosidases has been carried out.
Carmona Asenjo, Ana Teresa, Elías Rodríguez, María del Pilar, Ide, Daisuke, Kato, Atsushi, Miyawaki, Shota, Moreno Vargas, Antonio José, Pingitore, Valeria, Robina Ramírez, Inmaculada, Álvarez González, Eleuterio   +8 more
core   +1 more source

The Continuous Challenge of Diagnosing patients with Fabry disease in Argentina : Genotype, Experiences, Anecdotes, and New Learnings [PDF]

, 2015
The lysosomal storage disorder Fabry disease (FD) is caused by pathogenic mutations in the α-galactosidase A gene, localized in X chromosome. Deficient enzymatic activity of the product of this gene, the lysosomal hydrolase α-galactosidase A, leads to ...
Ceci, Romina, Kisinovsky, Isaac, Roa, Norma, Rozenfeld, Paula Adriana   +3 more
core   +5 more sources

Anaerobic expression of thegyrAgene demonstrated by β-galactosidase activity ingyrA::Mu-lacfusion derivatives ofEscherichia coli [PDF]

FEMS Microbiology Letters, 1988
E. coli C600Δ lac was infected with a Mu- lac defective phage. Lysogens resistant to ampicillin (25 µg/ml) and nalidixic acid (20 µg/ml) were unable to grow anaerobically and insensitive to nalidixic acid (150 µg/ml), indicating formation of gyrA ::Mu- lac fusions.
Nobuto Yamamoto, Mary L. Droffner
openaire   +1 more source