The effect of chemical modification of basic amino acid residues on the activation and amidolytic activity of Hageman factor (factor XII).
Modification of arginyl residues of Hageman factor by phenylglyoxal hydrate inhibits activation of this clotting factor in a plasma-free system, that is, in the absence of the other constituents of the contact activation system. Activation is also inhibited by alteration of the other two basic amino acid residues present, lysine and histidine. Chemical modification of histidine and arginine residues does not inhibit the amidolytic activity of activated Hageman factor. In contrast, modification of amino group(s) in N-terminal and lysine residues inhibits activated Hageman factor. Thus, basic amino acid residues essential to the activation or activity of Hageman factor appear to be variably accessible to chemical modification.
Ryder
J
J
Department of Pathology, School of Medicine, Case Western Reserve University Cleveland, OH.
Everson
B
B
Jentoft
J
J
Ratnoff
O D
OD
D000577:Amides / Q000378:metabolism; D000596:Amino Acids / Q000737:chemistry*; D001120:Arginine / Q000737:chemistry; D004047:Diethyl Pyrocarbonate / Q000494:pharmacology; D005174:Factor XII / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D015956:Factor XIIa / Q000378:metabolism; D006639:Histidine / Q000737:chemistry; D006801:Humans; D008239:Lysine / Q000737:chemistry; D010658:Phenylglyoxal / Q000494:pharmacology; D012710:Serum Albumin, Bovine / Q000494:pharmacology; D013329:Structure-Activity Relationship; D014302:Trinitrobenzenesulfonic Acid / Q000494:pharmacology
D000577:Amides; D000596:Amino Acids; D012710:Serum Albumin, Bovine; D006639:Histidine; D014302:Trinitrobenzenesulfonic Acid; D005174:Factor XII; D001120:Arginine; D015956:Factor XIIa; D008239:Lysine; D004047:Diethyl Pyrocarbonate; D010658:Phenylglyoxal