Irreversible inhibition of serine proteases by peptidyl derivatives of α-aminoalkylphosphonate diphenyl esters

Biochemical and Biophysical Research Communications

Volumn 161, Issue 1, 1989, Pages 143-149

  Oleksyszyn, Józef ^a   Powers, James C ^a  

^a GEORGIA INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHYMOTRYPSIN; ELASTASE; SERINE PROTEINASE;

1 AMINOALKYLPHOSPHONIC ACID DERIVATIVE; ENZYME INHIBITION; PRIORITY JOURNAL;

BINDING SITES; CHYMOTRYPSIN; ENZYME STABILITY; HUMAN; KINETICS; OLIGOPEPTIDES; ORGANOPHOSPHORUS COMPOUNDS; PANCREATIC ELASTASE; PEPTIDES; SERINE PROTEINASE INHIBITORS; SUBSTRATE SPECIFICITY; SUPPORT, U.S. GOV'T, P.H.S.;

EID: 0024341633     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/0006-291X(89)91572-6     Document Type: Article

References (17)

1. Inhibition of chymotrypsin by phosphonate and phosphonamidate peptide analogs
2. Diphenyl 1-Aminoalkanephosphonates
3. On the size of the active site in proteases. I. Papain