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4-nitrophenylgalactoside and glucose, (beta-d)-isomer

4-nitrophenylgalactoside has been researched along with glucose, (beta-d)-isomer in 6 studies

Research

Studies (6)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's3 (50.00)18.2507
2000's1 (16.67)29.6817
2010's2 (33.33)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Fukumura, M; Ohmiya, K; Sakka, K; Shimada, K1
Awazu, S; Hayashi, M; Mizuma, T; Ohta, K1
Akao, T; Hattori, M; Kobashi, K; Yang, L1
Hengstenberg, W; Schulte, D1
Cao, A; Liu, Y; Tang, Y1
Ashfaq, UA; Ehsan, B; Haq, A; Idrees, S; Rajoka, MI1

Other Studies

6 other study(ies) available for 4-nitrophenylgalactoside and glucose, (beta-d)-isomer

ArticleYear
Nucleotide sequence of the Clostridium stercorarium xynB gene encoding an extremely thermostable xylanase, and characterization of the translated product.
    Bioscience, biotechnology, and biochemistry, 1995, Volume: 59, Issue:1

    Topics: Amino Acid Sequence; Base Sequence; beta-Glucosidase; Clostridium; Electrophoresis, Polyacrylamide Gel; Enzyme Stability; Escherichia coli; Gene Expression Regulation, Enzymologic; Glucosides; Glycoside Hydrolases; Glycosides; Hot Temperature; Hydrogen-Ion Concentration; Molecular Sequence Data; Molecular Weight; Nitrophenylgalactosides; Promoter Regions, Genetic; Protein Biosynthesis; Restriction Mapping; Sequence Homology, Amino Acid; Sequence Homology, Nucleic Acid; Substrate Specificity; Xylan Endo-1,3-beta-Xylosidase; Xylosidases

1995
Comparative study of active absorption by the intestine and disposition of anomers of sugar-conjugated compounds.
    Biochemical pharmacology, 1993, Apr-06, Volume: 45, Issue:7

    Topics: Animals; Biological Transport; Glucosides; Intestinal Absorption; Male; Nitrophenylgalactosides; Prodrugs; Rats; Rats, Wistar; Time Factors

1993
A sennoside-hydrolyzing beta-glucosidase from Bifidobacterium sp. strain SEN is inducible.
    Biological & pharmaceutical bulletin, 1996, Volume: 19, Issue:5

    Topics: Anthraquinones; beta-Glucosidase; Bifidobacterium; Chloramphenicol; Enzyme Induction; Feces; Glucose; Glucosides; Humans; Nitrophenylgalactosides; RNA, Bacterial; Senna Extract; Sennosides; Substrate Specificity

1996
Engineering the active center of the 6-phospho-beta-galactosidase from Lactococcus lactis.
    Protein engineering, 2000, Volume: 13, Issue:7

    Topics: Amino Acid Substitution; Amino Acids; Bacterial Proteins; beta-Galactosidase; Binding Sites; Escherichia coli; Galactosephosphates; Glucosides; Glycoside Hydrolases; Lactococcus lactis; Models, Molecular; Mutagenesis, Site-Directed; Nitrophenylgalactosides; Protein Structure, Tertiary; Recombinant Fusion Proteins; Species Specificity; Substrate Specificity

2000
Novel fluorescent biosensor for α-glucosidase inhibitor screening based on cationic conjugated polymers.
    ACS applied materials & interfaces, 2012, Volume: 4, Issue:8

    Topics: alpha-Glucosidases; Biosensing Techniques; Cations; Diabetes Mellitus; Fluorenes; Fluorescent Dyes; Glucosides; Humans; Hydrolysis; Inhibitory Concentration 50; Kinetics; Nitrophenols; Nitrophenylgalactosides; Polymers; Quaternary Ammonium Compounds; Spectrophotometry

2012
Determination of substrate specificities against β-glucosidase A (BglA) from Thermotoga maritime: a molecular docking approach.
    Journal of microbiology and biotechnology, 2015, Volume: 25, Issue:1

    Topics: Amino Acid Sequence; Benzyl Alcohols; beta-Glucosidase; Cellobiose; Glucosides; Hydrogen Bonding; Hymecromone; Kinetics; Molecular Conformation; Molecular Docking Simulation; Nitrophenylgalactosides; Software; Substrate Specificity; Thermotoga maritima

2015