Purification, biochemical and functional characterization of miliin, a new thiol-dependent serine protease isolated from the latex of Euphorbia milii.
Miliin, a new thiol-dependent serine protease purified from the latex of Euphorbia milii possesses a molecular weight of 79 kDa, an isoelectric point of 4.3 and is optimally active at 60 degrees C in the pH range of and 7.5-11.0. Activity tests indicate that milliin is a thiol-dependent serine protease.
Moro
L P
LP
Department of Chemistry and Environmental Sciences, IBILCE-UNESP, São José do Rio Preto SP, Brazil.
Murakami
M T
MT
Cabral
H
H
Vidotto
A
A
Tajara
E H
EH
Arni
R K
RK
Juliano
L
L
Bonilla-Rodriguez
G O
GO
D004591:Electrophoresis, Polyacrylamide Gel; D028481:Euphorbia / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D007526:Isoelectric Point; D007700:Kinetics; D007840:Latex / Q000737:chemistry; D008970:Molecular Weight; D012697:Serine Endopeptidases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D013696:Temperature
D007840:Latex; D012697:Serine Endopeptidases