Compounds > glucose, (beta-d)-isomer
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glucose, (beta-d)-isomer and 3kb-cnp-beta-g5

glucose, (beta-d)-isomer has been researched along with 3kb-cnp-beta-g5 in 5 studies

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's4 (80.00)18.2507
2000's1 (20.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Hanayama, N; Ishimaru, K; Kamezono, Y1
Hayashi, Y; Ishimaru, K; Kamezono, Y; Teshima, S1
Emi, S; Hayashi, Y; Ishimaru, K; Teshima, S1
Haga, K; Nakamura, A; Yamane, K1
Fushinobu, S; Imamura, H; Jeon, BS; Matsuzawa, H; Wakagi, T1

Other Studies

5 other study(ies) available for glucose, (beta-d)-isomer and 3kb-cnp-beta-g5

ArticleYear
New method for preparing 3-ketobutylidene 2-chloro-4-nitrophenyl beta-maltopentaoside.
    Bioscience, biotechnology, and biochemistry, 1992, Volume: 56, Issue:7

    Topics: alpha-Amylases; Biotechnology; Carbohydrate Sequence; Glucosides; Magnetic Resonance Spectroscopy; Methods; Molecular Sequence Data; Substrate Specificity

1992
Enzymatic synthesis of 2-chloro-4-nitrophenyl 4,6-O-3-ketobutylidene beta-maltopentaoside, a substrate for alpha-amylase.
    Bioscience, biotechnology, and biochemistry, 1992, Volume: 56, Issue:10

    Topics: 1-Propanol; alpha-Amylases; Bacillus; Carbohydrate Sequence; Glucosides; Glucosyltransferases; Glycosylation; Molecular Sequence Data; Nitrobenzenes

1992
Determination of alpha-amylase using a new blocked substrate (3-ketobutylidene beta-2-chloro-4-nitrophenyl-maltopentaoside).
    Clinica chimica acta; international journal of clinical chemistry, 1991, May-31, Volume: 199, Issue:1

    Topics: alpha-Amylases; Chromatography, High Pressure Liquid; Glucosidases; Glucosides; Humans; Hydrogen-Ion Concentration; Indicators and Reagents; Kinetics; Pancreas; Saliva; Spectrophotometry, Ultraviolet; Substrate Specificity

1991
The transglycosylation reaction of cyclodextrin glucanotransferase is operated by a Ping-Pong mechanism.
    FEBS letters, 1994, Jan-03, Volume: 337, Issue:1

    Topics: Bacillus; Binding Sites; Carbohydrate Metabolism; Carbohydrates; Escherichia coli; Glucose; Glucosides; Glucosyltransferases; Glycosylation; Hydrolysis; Kinetics; Maltose; Molecular Conformation; Recombinant Proteins; Sorbose; Substrate Specificity; Xylose

1994
Identification of the catalytic residue of Thermococcus litoralis 4-alpha-glucanotransferase through mechanism-based labeling.
    Biochemistry, 2001, Oct-16, Volume: 40, Issue:41

    Topics: Amino Acid Sequence; Base Sequence; Carbohydrate Sequence; Catalytic Domain; Glucosides; Glycogen Debranching Enzyme System; Humans; Molecular Sequence Data; Mutagenesis, Site-Directed; Sequence Homology, Amino Acid; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Substrate Specificity; Thermococcus

2001