The Specific Inactivation of Trypsin by Ethyl p-Guanidinobenzoate

摘要: Abstract Ethyl p-guanidinobenzoate, which is closely related structurally to some aromatic esters split by trypsin, only a partial substrate for the enzyme. Kinetic evidence was obtained formation of typical enzyme-substrate complex which, however, proceeded stable acyl-enzyme derivative, even at pH normally optimal tryptic hydrolyses. The stoichiometry reaction established spectroscopic analysis. Trypsin consequently inactivated ethyl p-guanidinobenzoate. Under similar conditions, chymotrypsin unaffected. Difference spectra appearing during inactivation indicate transfer p-guanidinobenzoyl group from an aqueous hydrophobic environment, concomitant with analogous shift tyrosine residues trypsin. residue or may be involved in binding site active center. failure p-guanidinobenzoyltrypsin undergo deacylation attributed distortion hydrolytic