title: Cucumisin-like protease from the latex of Euphorbia supina.
abstract: A protease has been purified from the latex of Euphorbia supina Rafin by two steps of chromatography. The Mr was estimated by SDS-PAGE to be 80 kDa. Its activity was inhibited strongly by diisopropyl fluorophosphate, but not by EDTA, pepstatin, or cysteine protease inhibitors, indicating that the enzyme is a serine protease. The specificity of the protease is broad, but the preferential cleavage sites were C-terminal sites of hydrophobic amino acid residues. The N-terminal sequence of the first fifteen residues was determined and six of the residues match those in cucumisin [EC 3.4.21.25], a protease from the sarcocarp of melon fruit (Cucumis melo L. var. Prince). The results indicate that the E. supina protease is a cucumisin-like serine protease.
authors.affiliation: Department of Chemistry, Faculty of Science, Kagoshima University, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Arima
authors.forename: T
authors.initials: T
authors.lastname: Uchikoba
authors.forename: H
authors.initials: H
authors.lastname: Yonezawa
authors.forename: M
authors.initials: M
authors.lastname: Shimada
authors.forename: M
authors.initials: M
authors.lastname: Kaneda
mesh_terms: D000595:Amino Acid Sequence; D002845:Chromatography; D004591:Electrophoresis, Polyacrylamide Gel; D019665:Euphorbiaceae / Q000737:chemistry*; D007840:Latex / Q000737:chemistry*; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000737:chemistry / Q000302:isolation & purification*
chemical_list: D007840:Latex; D012697:Serine Endopeptidases; C411338:protease B, Euphorbia supina; C041541:cucumisin