bromochloroacetic-acid has been researched along with epsilon-(gamma-glutamyl)-lysine* in 2 studies
2 other study(ies) available for bromochloroacetic-acid and epsilon-(gamma-glutamyl)-lysine
| Article | Year |
|---|---|
Role of transglutaminase in keratinization of vaginal epithelial cells in oestrous cycling rats.
Aspects of the regulation of calcium dependent transglutaminase (TGase) enzyme in the terminally differentiating vaginal epithelial cells (VEC) from cycling and oestradiol primed ovariectomized (OVX) rats are described. There is a significant increase in the TGase activity and a quantitative rise in its cross-linked sigma(tau-glutamyl)lysine covalent product in the VEC of oestrus rats. A similar phenomena was also evident in the oestradiol primed OVX rats. However, in the VEC of the diestrus/unprimed OVX rats, the enzyme activity and its cross-linked product tend to be at its basal level. An increase of TGase activity in the keratinized layers of the oestrus VEC was observed. Immunohistochemical localization data parallel the biochemical measurements. These findings suggest that TGase activity may be associated with the differential status of the cell and primarily aids in the conferring structural stability and integrity to the stratified VEC. Aggregates of the keratin tonofilament bundles which are covalently cross-linked by the formation of sigma(tau-glutamyl)lysine in the oestrus vagina renders them resistant to denaturant and proteolytic treatments. Topics: Animals; Calcium; Dipeptides; Enzyme Activation; Epithelial Cells; Estrus; Female; Immunoblotting; Immunohistochemistry; Intracellular Fluid; Keratins; Lysine; Rats; Rats, Wistar; Transglutaminases; Vagina | 1997 |
Quantitation of the epsilon-(gamma-glutamyl)lysine cross-link using a high-speed amino acid analyzer without purification of the dipeptide. Application to enzymatic digested mixtures of keratin and the membranous fraction of human stratum corneum.
epsilon-(gamma-Glutamyl)lysine in an enzymically digested mixture of keratin and the membranous fraction of human stratum corneum was directly quantitated using a high-speed amino acid analyzer without purification of the dipeptide. The analytical conditions were improved so that epsilon-(gamma-glutamyl)lysine clearly separated from other amino acids and eluted directly after tyrosine. The enzymatically digested mixtures were filtered through an Ultra Free membrane and deammoniated before analysis. By our present method, keratin and the membranous fraction of human stratum corneum were analyzed and 5.8 and 43.5 nmol/mg of epsilon-(gamma-glutamyl)lysine, respectively, were detected. Topics: Amino Acids; Autoanalysis; Chromatography, Ion Exchange; Dipeptides; Enzymes; Humans; Keratins; Methods; Skin | 1983 |