Arginines analysis

Acetylimidazole 95 acrylonitrile 112 affinity labels 135 amide content 18,21 amidination 69 amino acid analysis 13 aminopeptidase M 39, 42 diketopiperazines 42 amino-terminal sequences 59 arginine analysis 37... 

ENZYMATIC ANALYSIS WITH CARBOXYPEPTIDASES. Carboxypeptidases are enzymes that cleave amino acid residues from the C-termini of polypeptides in a successive fashion. Four carboxypeptidases are in general use A, B, C, and Y. Carboxypeptidase A (from bovine pancreas) works well in hydrolyzing the C-terminal peptide bond of all residues except proline, arginine, and lysine. The analogous enzyme from hog pancreas, carboxypeptidase B, is effective only when Arg or Lys are the C-terminal residues. Thus, a mixture of carboxypeptidases A and B liberates any C-terminal amino acid except proline. Carboxypeptidase C from citrus leaves and carboxypeptidase Y from yeast act on any C-terminal residue. Because the nature of the amino acid residue at the end often determines the rate at which it is cleaved and because these enzymes remove residues successively, care must be taken in interpreting results. Carboxypeptidase Y cleavage has been adapted to an automated protocol analogous to that used in Edman sequenators. 

Cotham WE, Metz TO, Ferguson PL, et al. Proteomic analysis of arginine adducts on glyoxal-modified ribonuclease. Mol. Cell. Proteomics 2004 3 1145-1153. 

Scheer, A., Costa, T., Fanelli, F., et al. (2000) Mutational analysis of the highly conserved arginine within the Glu/Asp-Arg-Tyr motif of the alpha) lb)-adrenergic receptor effects on receptor isomerization and activation. Mol. Pharmacol. 57,219-231. 

For the residue-type assignment of the cross peaks, the SH3 domain was expressed with specifically labeled glycine or arginine residues by using amino acid mixtures where only Gly and Arg were 15N-labeled. Again, yields for the labeled proteins were identical to those of the unlabeled product. Analysis of the corresponding [15N,1H]-HSQC spectra... 

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