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glyceraldehyde/zubný kaz
Odkaz sa uloží do schránky
Strana 1 od 37 výsledky
Unfolded, oxidized, and thermoinactivated forms of glyceraldehyde-3-phosphate dehydrogenase interact with the chaperonin GroEL in different ways.
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The interaction of GroEL with different denatured forms of glyceraldehyde-3-phosphate dehydrogenase* (GAPDH) has been investigated. GroEL does not prevent thermal denaturation of GAPDH, but effectively interacts with the thermodenatured enzyme, thus preventing the aggregation of denatured molecules.
The crystal structure of the allosteric non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeum Thermoproteus tenax.
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The NAD(+)-dependent non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) from the hyperthermophilic archaeum Thermoproteus tenax represents an archaeal member of the diverse superfamily of aldehyde dehydrogenases (ALDHs). GAPN catalyzes the irreversible oxidation of d-glyceraldehyde
Cloning, characterization and DNA immunization of an Onchocerca volvulus glyceraldehyde-3-phosphate dehydrogenase (Ov-GAPDH).
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In the search for Onchocerca volvulus antigens possibly involved in protection against human onchocerciasis, partial amino acid sequence analysis of one of the O. volvulus antigens of the serologically identified proteins showed a close relationship to the glyceraldehyde-3-phosphate dehydrogenase
[Experimental study of glyceraldehyde cross-linking of posterior scleral on FDM in guinea pigs].
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OBJECTIVE
The purpose of this study is to observe the effects of glyceraldehyde cross-linking on sclera biomechanical strength and experimental myopia.
METHODS
50 three weeks aged guinea pigs were randomly divided into 5 groups: A, B, C, D, E. Each group had 10 guinea pigs. The right eye was set as
pH-regulated secretion of a glyceraldehyde-3-phosphate dehydrogenase from Streptococcus gordonii FSS2: purification, characterization, and cloning of the gene encoding this enzyme.
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Streptococcus gordonii and other viridans streptococci (VS) are primary etiologic agents of infective endocarditis, despite being part of the normal oral microflora. Recently, a surface-bound glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has been found on the cells of all tested streptococcal
Formation of homo- and heterooligomeric supramolecular structures by D-glyceraldehyde-3-phosphate dehydrogenase and lactate dehydrogenase in reversed micelles of aerosol OT in octane.
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The supramolecular structure of oligomeric enzymes can be specifically regulated by changing the size of an inner cavity of Aerosol OT reversed micelles in octane. Both D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and lactate dehydrogenase (LDH) reveal an ability to exist and function in
Conformational changes in Leishmania mexicana glyceraldehyde-3-phosphate dehydrogenase induced by designed inhibitors.
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The glycolytic enzymes of trypanosomes are attractive drug targets, since the blood-stream form of Trypanosoma brucei lacks a functional citric acid cycle and is dependent solely on glycolysis for its energy requirements. Glyceraldehyde-3-phosphate dehydrogenases (GAPDH) from the pathogenic
Glycine to alanine substitutions in helices of glyceraldehyde-3-phosphate dehydrogenase: effects on stability.
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Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from chicken was expressed in and purified from Escherichia coli. To investigate the physical basis of possible protein stabilization strategies, the effect of substitutions of glycine residues by alanine in helical regions was determined. One Gly to
Identification of the binding domain of Streptococcus oralis glyceraldehyde-3-phosphate dehydrogenase for Porphyromonas gingivalis major fimbriae.
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Porphyromonas gingivalis forms communities with antecedent oral biofilm constituent streptococci. P. gingivalis major fimbriae bind to glyceraldehyde-3-phosphate dehydrogenase (GAPDH) present on the streptococcal surface, and this interaction plays an important role in P. gingivalis colonization.
Identification of glyceraldehyde-3-phosphate dehydrogenase of epithelial cells as a second molecule that binds to Porphyromonas gingivalis fimbriae.
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Binding of Porphyromonas gingivalis to the host cells is an essential step in the pathogenesis of periodontal disease. P. gingivalis binds to and invades epithelial cells, and fimbriae are thought to be involved in this process. In our earlier studies, two major epithelial cell components of 40 and
Effect of matrix composition and process conditions on casein-gelatin beads floating properties.
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Casein-gelatin beads have been prepared by emulsification extraction method and cross-linked with D,L-glyceraldehyde in an acetone-water mixture 3:1 (v/v). Casein emulsifying properties cause air bubble incorporation and the formation of large holes in the beads. The high porosity of the matrix
A shared binding site for NAD+ and coenzyme A in an acetaldehyde dehydrogenase involved in bacterial degradation of aromatic compounds.
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The meta-cleavage pathway for catechol is a central pathway for the bacterial dissimilation of a wide variety of aromatic compounds, including phenols, methylphenols, naphthalenes, and biphenyls. The last enzyme of the pathway is a bifunctional aldolase/dehydrogenase that converts
[Ultrastructural demonstration of the human papilloma virus (HPV) in oral proliferative lesions].
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The Human Papilloma Virus (HPV) has been found in a series of benign proliferative lesions of the skin and mucosa. The virus has also been found in verrucous laryngeal carcinoma and carcinomas of the oral cavity and other organs. DNA hybridization techniques have made it possible to classify 51
1.7 A structure of FR-1, a fibroblast growth factor-induced member of the aldo-keto reductase family, complexed with coenzyme and inhibitor.
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Murine FR-1 is a protein that is induced by fibroblast growth factor-1 and, therefore, may play a role in the regulation of the cell cycle. Sequence comparison indicates that it is a member of the NADPH-dependent aldo-keto reductase family. It bears 70% identity to human aldose reductase, an enzyme
Antimicrobial actions of benzimidazoles against oral streptococci.
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OBJECTIVE
Benzimidazoles, such as lansoprazole and omeprazole, are used extensively as proton-pump inhibitors to control stomach acid secretion and also have antimicrobial actions against Helicobacter pylori. Our objective was to determine whether they are potentially useful antimicrobials against
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