Histidine-rich glycoprotein (HRG) is a plasma protein consisting of 6 distinct functional domains and is an important regulator of key cardiovascular processes, including angiogenesis and coagulation. The protein is composed of 2 N-terminal domains (N1 and N2), 2 proline-rich regions (PRR1 and PRR2) that flank a histidine-rich region (HRR), and a C-terminal domain. To date, structural informati...

Diglycyl-L-histidine is a peptide molecule designed to mimic the specific Cu(II) transport site of human albumin. The equilibria involved in the Cu(II)-diglycyl-L-histidine system have been investigated by analytical potentiometry in aqueous solution (0.15 M NaCl, 25’). The synthetic peptide molecule bound Cu(I1) exclusively as a 1: I complex in the pH range of 6.50 to 11.00. The results furthe...

The stability constants of species present in the systems Ni(II)-pyridoxamine(pym)(A) and Ni(II)-pyridoxamine(pym)(A)-imidazole containing ligands(B) [B = imidazole(him),  benzimidazole(bim), histamine(hist) and L-histidine(his)] have been determined pH-metrically using the MINIQUAD computer program. The existence of the species NiAH, NiA and NiA2 was proven for the Ni(II)-pym(A)...

Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) is a universally used method for determining approximate molecular weight (MW) in protein research. Migration of protein that does not correlate with formula MW, termed "gel shifting" appears to be common for histidine-rich proteins but not yet studied in detail. We investigated "gel shifting" in Ni2+-binding histidine-rich H...

Diglycyl-L-histidine is a peptide molecule designed to mimic the specific Cu(II) transport site of human albumin. The equilibria involved in the Cu(II)-diglycyl-L-histidine system have been investigated by analytical potentiometry in aqueous solution (0.15 M NaCl, 25’). The synthetic peptide molecule bound Cu(I1) exclusively as a 1: I complex in the pH range of 6.50 to 11.00. The results furthe...