L-Lysine, N6-formyl-
L-Lysine, N6-formyl- structure
|
Common Name | L-Lysine, N6-formyl- | ||
|---|---|---|---|---|
| CAS Number | 1190-48-3 | Molecular Weight | 174.19800 | |
| Density | 1.169g/cm3 | Boiling Point | 438.5ºC at 760mmHg | |
| Molecular Formula | C7H14N2O3 | Melting Point | N/A | |
| MSDS | USA | Flash Point | 219ºC | |
|
Analysis of glycated and ascorbylated proteins by gas chromatography-mass spectrometry.
J. Agric. Food Chem. 50 , 5697-5703, (2002) Proteins or poly-L-lysine which were incubated in the presence of ascorbic acid, dehydroascorbic acid (ascorbylation), or various sugars (glycation) were analyzed by gas chromatography-mass spectrometry (GC-MS). To also detect more labile reaction products, t... |
|
|
The isolation of Nepsilon-formyl-L-lysine from the reaction between formaldehyde and L-lysine and its identification by OPLC and NMR spectroscopy.
J. Pharm. Biomed. Anal. 3 , 343-349, (1985) From the reaction between l-lysine and formaldehyde, Nepsilon-formyl-L-lysine was isolated by means of ion-exchange column chromatography. The identification of Nepsilon-formyl-L-lysine was carried out by ion-exchange overpressured-layer chromatography (OPLC)... |
|
|
Quantitative analysis of histone modifications: formaldehyde is a source of pathological n(6)-formyllysine that is refractory to histone deacetylases.
PLoS Genet. 9(2) , e1003328, (2013) Aberrant protein modifications play an important role in the pathophysiology of many human diseases, in terms of both dysfunction of physiological modifications and the formation of pathological modifications by reaction of proteins with endogenous electrophi... |
|
|
Cleavage by trypsin and by the proteinase from Armillaria mellea at epsilon-N-formyl-lysine residues.
Biochem. J. 193(3) , 737-42, (1981) Kinetic studies were made of the hydrolysis by trypsin of alpha-N-acetylglycyl-L-lysine methyl ester and of its neutral analogue alpha-N-acetylglycyl-epsilon-N-formyl-L-lysine methyl ester. The latter substance is a moderately good substrate for trypsin, and ... |