L-Histidine is a natural proteinogenic α amino acid useful as a cell growth supplement that support protein and peptide biosynthesis. L-Histidine is studied in a wide range of applications that involve imidazole chemistry and biochemisty.
L-Histidine is a positively charged imidazole-side chain containing α amino acid. It is metabolized to histamine and is a precursor of the dipeptide carnosine. As one of the 22 proteinogenic amino acids L-His is incorporated into proteins by translation processes in vitro. L-Histidine is an essential amino acid added to cell culture media.
Analytical and bioanalytical chemistry, 399(8), 2779-2794 (2011-02-01)
The radical oxidation of isomeric peptides containing one reactive amino acid [histidine (H)] and another less reactive amino acid [glycine (G)] in the form of dipeptides (HG and GH) and tripeptides (HGG, GHG, and GGH) was studied by mass spectrometry
Seminars in thrombosis and hemostasis, 37(4), 389-394 (2011-08-02)
Histidine-rich glycoprotein (HRG) is one of the major plasma proteins and thought to function in blood coagulation, fibrinolysis, and innate immune systems. The amino acid sequence of HRG revealed a multidomain structure consisting of cystatin-like domains 1 and 2, a
Current opinion in microbiology, 15(2), 118-124 (2011-12-17)
Two-component systems, composed of a histidine kinase (HK) and a response regulator (RR), are the major signal transduction devices in bacteria. Originally it was thought that these two components function as linear, phosphorylation-driven stimulus-response system. Here, we will review how
Indian journal of pharmacology, 45(2), 126-129 (2013-05-30)
Cyclophosphamide (CP), a widely used antineoplastic drug causes hemorrhagic cystitis (HC) mainly via induction of oxidative stress. Both vitamin C and histidine have antioxidant properties. The present study aimed to investigate the effects of oral (p.o.) administration of vitamin C
Proceedings of the National Academy of Sciences of the United States of America, 108(14), 5602-5607 (2011-03-23)
A method is proposed to determine the fraction of the tautomeric forms of the imidazole ring of histidine in proteins as a function of pH, provided that the observed and chemical shifts and the protein structure, or the fraction of
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