title: Purification, biochemical and functional characterization of miliin, a new thiol-dependent serine protease isolated from the latex of Euphorbia milii.
abstract: 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.
authors.affiliation: Department of Chemistry and Environmental Sciences, IBILCE-UNESP, São José do Rio Preto SP, Brazil.
authors.forename: L P
authors.initials: LP
authors.lastname: Moro
authors.forename: M T
authors.initials: MT
authors.lastname: Murakami
authors.forename: H
authors.initials: H
authors.lastname: Cabral
authors.forename: A
authors.initials: A
authors.lastname: Vidotto
authors.forename: E H
authors.initials: EH
authors.lastname: Tajara
authors.forename: R K
authors.initials: RK
authors.lastname: Arni
authors.forename: L
authors.initials: L
authors.lastname: Juliano
authors.forename: G O
authors.initials: GO
authors.lastname: Bonilla-Rodriguez
mesh_terms: 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
chemical_list: D007840:Latex; D012697:Serine Endopeptidases