ethyldimethylaminopropyl carbodiimide has been researched along with acetylglucosamine in 4 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 1 (25.00) | 18.7374 |
1990's | 3 (75.00) | 18.2507 |
2000's | 0 (0.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Gooday, GW; Milewski, S; O'Donnell, RW | 1 |
Huynh, QK; Lisek, CA; Smith, CE; Verburg, JG | 1 |
Imoto, T; Kuroki, R; Yamada, H | 1 |
Funatsu, G; Yamagami, T | 1 |
4 other study(ies) available for ethyldimethylaminopropyl carbodiimide and acetylglucosamine
Article | Year |
---|---|
Chemical modification studies of the active centre of Candida albicans chitinase and its inhibition by allosamidin.
Topics: Acetylglucosamine; Aspartic Acid; Binding Sites; Binding, Competitive; Candida albicans; Chitinases; Diethyl Pyrocarbonate; Ethyldimethylaminopropyl Carbodiimide; Glutamates; Glutamic Acid; Kinetics; Phenylglyoxal; Sulfhydryl Reagents; Trisaccharides | 1992 |
Identification of an essential tyrosine residue in the catalytic site of a chitinase isolated from Zea mays that is selectively modified during inactivation with 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide.
Topics: Acetylglucosamine; Amino Acid Sequence; Binding Sites; Chitinases; Chromatography, High Pressure Liquid; Ethyldimethylaminopropyl Carbodiimide; Iodoacetamide; Kinetics; Mass Spectrometry; Molecular Sequence Data; Muramidase; Sequence Alignment; Sequence Homology, Nucleic Acid; Trypsin; Tyrosine; Zea mays | 1992 |
Specific carbodiimide-binding mechanism for the selective modification of the aspartic acid-101 residue of lysozyme in the carbodiimide-amine reaction.
Topics: Acetylglucosamine; Amines; Aspartic Acid; Binding Sites; Binding, Competitive; Carbodiimides; Chromatography, High Pressure Liquid; Chromatography, Ion Exchange; Ethanolamine; Ethanolamines; Ethyldimethylaminopropyl Carbodiimide; Mathematics; Muramidase; Oxidation-Reduction; Polymers; Protein Binding; Sodium Chloride; Tryptophan | 1986 |
Identification of the aspartic acid residue located at or near substrate-binding site of rye seed chitinase-c.
Topics: Acetylglucosamine; Amino Acid Sequence; Aspartic Acid; Binding Sites; Chitinases; Chromatography, High Pressure Liquid; Chymotrypsin; Cross-Linking Reagents; Ethyldimethylaminopropyl Carbodiimide; Glycine; Molecular Sequence Data; Secale; Seeds; Sequence Alignment; Spectrophotometry, Ultraviolet; Trypsin | 1998 |