Copper-Catalyzed Electrochemical Chlorination of 1,3-Dicarbonyl Compounds Using Hydrochloric Acid

2013 ◽  
Vol 2 (11) ◽  
pp. 935-937 ◽  
Author(s):  
Kazuya Tsuchida ◽  
Takuya Kochi ◽  
Fumitoshi Kakiuchi
Keyword(s):  
Hydrochloric Acid ◽  
Dicarbonyl Compounds ◽  
Electrochemical Chlorination

A simple and effective method for the reduction of acyl substituted heterocyclic 1,3-dicarbonyl compounds to alkyl derivatives by zinc - acetic acid - hydrochloric acid

Tetrahedron ◽  
1995 ◽  
Vol 51 (47) ◽  
pp. 12923-12928 ◽  
Author(s):  
Thomas Kappe ◽  
Rudolf Aigner ◽  
Peter Roschger ◽  
Barbara Schnell ◽  
Wolfgang Stadibauer
Keyword(s):  
Acetic Acid ◽  
Hydrochloric Acid ◽  
Dicarbonyl Compounds ◽  
Alkyl Derivatives

Preparation of iodonium ylides: probing the fluorination of 1,3-dicarbonyl compounds with a fluoroiodane

RSC Advances ◽  
2015 ◽  
Vol 5 (21) ◽  
pp. 16501-16506 ◽  
Author(s):  
Gemma C. Geary ◽  
Eric G. Hope ◽  
Kuldip Singh ◽  
Alison M. Stuart
Keyword(s):  
Acetic Acid ◽  
Hydrochloric Acid ◽  
Dicarbonyl Compounds ◽  
Toluenesulfonic Acid ◽  
Iodonium Ylides

The isolated iodonium ylide has been reacted successfully with TREAT-HF, hydrochloric acid, acetic acid and p-toluenesulfonic acid to form the 2-fluoro-, 2-chloro-, 2-acetyl- and 2-tosyl-1,3-ketoesters respectively.

Fine Structure of Platelet Interaction with a New Microcrystalline Collagen Preparation

1974 ◽  
Vol 32 ◽  
pp. 58-59
Author(s):  
W. H. Zucker ◽  
R. G. Mason
Keyword(s):  
Fine Structure ◽  
Platelet Aggregation ◽  
Hydrochloric Acid ◽  
Whole Blood ◽  
Platelet Adhesion ◽  
Hemostatic Agent ◽  
Native Collagen ◽  
Fibrillar Morphology ◽  
Clinical Interest ◽  
New Form

Platelet adhesion initiates platelet aggregation and is an important component of the hemostatic process. Since the development of a new form of collagen as a topical hemostatic agent is of both basic and clinical interest, an ultrastructural and hematologic study of the interaction of platelets with the microcrystalline collagen preparation was undertaken.In this study, whole blood anticoagulated with EDTA was used in order to inhibit aggregation and permit study of platelet adhesion to collagen as an isolated event. The microcrystalline collagen was prepared from bovine dermal corium; milling was with sharp blades. The preparation consists of partial hydrochloric acid amine collagen salts and retains much of the fibrillar morphology of native collagen.

Dicarbonyl derived post-translational modifications: chemistry bridging biology and aging-related disease

2020 ◽  
Vol 64 (1) ◽  
pp. 97-110
Author(s):  
Christian Sibbersen ◽  
Mogens Johannsen
Keyword(s):  
Mass Spectrometry ◽  
Future Research ◽  
Amino Acid Residues ◽  
Post Translational Modification ◽  
Dicarbonyl Compounds ◽  
Protein Targets ◽  
Post Translational Modifications ◽  
Reactive Protein ◽  
Glycation End Products ◽  
Direct Mass Spectrometry

Abstract In living systems, nucleophilic amino acid residues are prone to non-enzymatic post-translational modification by electrophiles. α-Dicarbonyl compounds are a special type of electrophiles that can react irreversibly with lysine, arginine, and cysteine residues via complex mechanisms to form post-translational modifications known as advanced glycation end-products (AGEs). Glyoxal, methylglyoxal, and 3-deoxyglucosone are the major endogenous dicarbonyls, with methylglyoxal being the most well-studied. There are several routes that lead to the formation of dicarbonyl compounds, most originating from glucose and glucose metabolism, such as the non-enzymatic decomposition of glycolytic intermediates and fructosyl amines. Although dicarbonyls are removed continuously mainly via the glyoxalase system, several conditions lead to an increase in dicarbonyl concentration and thereby AGE formation. AGEs have been implicated in diabetes and aging-related diseases, and for this reason the elucidation of their structure as well as protein targets is of great interest. Though the dicarbonyls and reactive protein side chains are of relatively simple nature, the structures of the adducts as well as their mechanism of formation are not that trivial. Furthermore, detection of sites of modification can be demanding and current best practices rely on either direct mass spectrometry or various methods of enrichment based on antibodies or click chemistry followed by mass spectrometry. Future research into the structure of these adducts and protein targets of dicarbonyl compounds may improve the understanding of how the mechanisms of diabetes and aging-related physiological damage occur.

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