Analyses of Reducing Sugars on a Thin-layer Chromatographic Plate with Modified Somogyi and Nelson Reagents, and with Copper Bicitichoninate
スポンサーリンク
概要
- 論文の詳細を見る
Two novel methods to detect reducing sugar on a thin-layer chromatographic plate, using aqueous coloring reagents and a commercial microwave oven, were developed. After spraying the modified Somogyi reagent on the plate, irrigating the reducing sugars, and then heating in a commercial microwave oven for a few minutes, the modified Nelson reagent was sprayed on the plates. Reducing sugars were only apparent as blue spots. On the other hand, after spraying the bicinchoninate reagent on the plates and then heating in the microwave oven, the sugar spots became reddish-violet. These two new methods enabled 0.1μg of glucose per spot to be detected on a TLC plate. Non-reducing sugars (sucrose, trehalose, methyl α-D-glucoside, and transfer products containing non-reducing ends) were not detectable by these methods.
- 社団法人日本農芸化学会の論文
- 1996-04-23
著者
-
Kim Yeon-kye
Department Of Applied Biological Science Faculty Of Agriculture Tokyo University Of Agriculture And
-
SAKANO Yoshiyuki
Department of Applied Biological Science, Tokyo University of Agriculture Technology
-
Sakano Yoshiyuki
Department Of Applied Biological Science Faculty Of Agriculture Tokyo University Of Agriculture And
-
Sakano Yoshiyuki
Department Of Applied Biological Science Faculty Of Agriculture Tokyo University Of Agriculture And
-
SAKANO Yoshiyuki
Department of Agricultural Chemistry, Faculty of Agriculture, Tokyo Noko University
関連論文
- Structures of Thermoactinomyces vulgaris R-47 α-Amylase II Complexed with Substrate Analogues
- The Deletion of Amino-Terminal Domain in Thermoactinomyces vulgaris R-47 α-Amylases : Effects of domain N on Activity, Specificity, Stability and Dimerization
- Analysis of Catalytic Residues of Thermoactinomyces vulgaris R-47 α-Amylase II (TVA II) by Site-directed Mutagenesis
- Subsite Structure of α-Amylase II from Thermoactinomyces vulgaris R-47
- Purification, Characterization, and Subsite Affinities of Thermoactinomyces vulgaris R-47 Maltooligosaccharide-metabolizing Enzyme Homologous to Glucoamylases
- Construction of an Efficient Expression System for Aspergillus Isopullulanase in Pichia pastoris, and a Simple Purification Method(Biochemistry & Molecular Biology)
- Reddish Escherichia coli Cells Caused by Overproduction of Bacillus stearothermophilus Uroporphyrinogen III Methylase : Cloning, Sequencing, and Expression of the Gene
- A Neopullulanase-type α-Amylase Gene from Thermoactinomyces vulgaris R-47
- Enzymatic Preparation of Novel Non-reducing Oligosaccharides Having an Isomaltosyl Residue by Using the Transfer Action of Isomaltodextranase from Arthrobacter globiformis T6
- Analyses of Reducing Sugars on a Thin-layer Chromatographic Plate with Modified Somogyi and Nelson Reagents, and with Copper Bicitichoninate
- Selection of an RNA Molecule That Specifically Inhibits the Protease Activity of Subtilisin
- Molecular Cloning and Characterization of an Enzyme Hydrolyzing p-Nitrophenyl α-D-Glucoside from Bacillus stearothermophilus SA0301
- Two Components of Cell-bound Isopullulanase from Aspergillus niger ATCC 9642 : Their Purification and Enzymatic Properties
- Hydrolysis of α-1, 6-Glucosidic Linkages by an α-Amylase from Thermoactinomyces vulgaris R-47
- Subsite Structure and Action Mode of the α-Amylase from Thermoactinomyces vulgaris
- Enzymatic Properties and Action Patterns of Thermoactinomyces vulgaris α-Amylase
- Studies on the Hydrolyzing Mechanism for Cyclodextrins of Thermoactinomyces vulgaris R-47 .ALPHA.-Amylase 2(TVAII). X-Ray Structure of the Mutant E354A Complexed with .BETA.-Cyclodextrin, and Kinetic Analyses on Cyclodextrins.