The reaction of penicillin with proteins.
The mode of reaction of benzylpenicillin with two proteins was studied, with particular reference to the allergenicity of penicillin. These reactions, with pig insulin, and with hen's-egg-white lysozyme, were carried out in neutral solution at 37 degrees C. High concentrations of penicillin are needed to label the proteins, owing to concurrent hydrolysis of penicillin. Evidence has been obtained that the penicillin-reactive sites on the insulin molecule are the alpha-amino group at the N-terminus of the A chain and the epsilon-amino group of the lysine residue; whereas a site of reaction with lysozyme appears to be the epsilon-amino group of lysine-116.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D002645:Chickens; D004342:Drug Hypersensitivity; D004529:Egg White; D006801:Humans; D007328:Insulin; D007700:Kinetics; D009113:Muramidase; D010400:Penicillin G; D010446:Peptide Fragments / Q000032:analysis; D011485:Protein Binding; D013552:Swine
D000596:Amino Acids; D007328:Insulin; D010446:Peptide Fragments; D009113:Muramidase; D010400:Penicillin G