Hydrolysis of Lysine Peptides by Plasmin

抄録

The syntheses of L-leucyl-L-lysine amide, glycyl-L-lysyl-L-lysine, glycyl-L-lysyl-L-lysine amide, glycyl-L-lysyl-L-arginine and L-lysyl-L-lysyl-L-arginine were described. All dipeptides and dipeptide amides examined were resistant to plasmin, while glycyl-L-lysine amide and L-leucyl-L-lysine amide were cleaved by trypsin although dipeptides were not. Tetrapeptide, glycyl-L-lysyl-L-lysyl-L-arginine, was hydrolyzed by plasmin to glycyl-L-lysine and L-lysyl-L-arginine, as well as by trypsin. L-Lysyl-L-lysyl-L-arginine was cleaved on lysyllysine bond by plasmin, however, no reaction occurred by trypsin. The other hand, L-lysyl-L-lysyl-L-lysine was hydrolyzed by trypsin to L-lysyl-L-lysine and L-lysine, although this tripeptide was not attacked by plasmin. Also glycyl-L-lysyl-L-lysine amide was not to be the substrate for plasmin, while this amide was attacked by trypsin, yielding glycyl-L-lysine and L-lysine amide in addition, to glycyl-L-lysyl-L-lysine, ammonia and L-lysine.