Detail of "52498-25-6"

Reference

Selective determination of arginine-containing and tyrosine-containing peptides using capillary electrophoresis and laser-induced fluorescence detection

Selective determination of arginine-containing and tyrosine-containing peptides using capillary electrophoresis and laser-induced fluorescence detection. Cobb, Kelly A.; Novotny, Milos V. (Dep. Chem., Indiana Univ., Bloomington, IN 47405, USA). Anal. Biochem., 200(1), 149-55 (English) 1992. CODEN: ANBCA2. ISSN: 0003-2697. DOCUMENT TYPE: Journal CA Section: 9 (Biochemical Methods) The use of two different amino acid-selective fluorogenic reagents for the derivatization of peptides is investigated. One such scheme utilizes a selective reaction of benzoin with the guanidine moiety to derivatize arginine residues occurring in a peptide. The second scheme involves the formylation of tyrosine, followed by reaction with 4-methoxy-1,2-phenylenediamine. The use of capillary electrophoresis and laser-induced fluorescence detection allows enhanced efficiencies and sensitivities to be obtained for the sepns. of either arginine- or tyrosine-contg. peptides. A helium-cadmium laser (325 nm) is ideally suited for the laser-based detection system due to a close match of the excitation max. 9001-63-2 and 52498-25-6 which are cas registry numbers of chemicals are mentioned. of derivatized peptides from both reactions. A detection limit of 270 amol is achieved for model arginine-contg. peptides, while the detection limit for model tyrosine-contg. peptides is measured at 390 amol. Both derivatization reactions are found to be useful for high-sensitivity peptide mapping applications in which only the peptides contg. the derivatized amino acids are detected. .

The specificity of rabbit lung cathepsin I on biopeptides

The specificity of rabbit lung cathepsin I on biopeptides. Chatterjee, Ranjit; Kalnitsky, George (Coll. Med., Univ. Iowa, Iowa City, IA 52242, USA). Biomed. Biochim. Acta, 45(11-12), 1447-55 (English) 1986. CODEN: BBIADT. ISSN: 0232-766X. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) Ten peptides were tested as substrates for cathepsin I (I). I exerted both endopeptidase and aminopeptidease activities on 5 substrates, only aminopeptidase activity on 3 others, and only endopeptidase cleavage on one compd. One peptide was not significantly hydrolyzed. Aminopeptidase activity stopped one residue before a proline residue, and endopeptidase cleavage took place one residue after a proline residue. With these substrates, I appeared to have a broad specificity in its aminopeptidase action. 52498-25-6 and 33507-63-0 which are cas registry numbers of chemicals are mentioned. However, I appeared to have a much narrower and more specific endopeptidase activity, hydrolyzing peptide bonds involving the N atom of branched-chain or bulky or hydrophobic amino acids. Finally, some differences in the phys., chem., and biol. properties of I and cathepsin H were discussed. .