Purification and partial characterization of a thiol proteinase inhibitor from Enterolobium contortisiliquum beans.
A thiol proteinase inhibitor was purified from Enterolobium contortisiliquum beans by affinity chromatography on carboxy-methylated-papain-Sepharose. The inhibitor represents a single polypeptide chain with a molecular mass of 60 kDa and inactivates papain (Ki = 0.58 x 10(-9) M) and bromelain. The inhibitor shows activity in the pH range 2 to 10 and at temperatures up to 60 degrees C.
Oliva
M L
ML
Centro Universitário de Corumbá, UFMS, Corumbá, Brazil.
Sampaio
M U
MU
Sampaio
C A
CA
D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D007887:Fabaceae / Q000201:enzymology*; D007700:Kinetics; D010206:Papain / Q000037:antagonists & inhibitors; D010946:Plants, Medicinal; D011480:Protease Inhibitors / Q000032:analysis / Q000302:isolation & purification*
D011480:Protease Inhibitors; D010206:Papain