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- Title
A Cysteine Protease Isolated from the Latex of Ficus microcarpa: Purification and Biochemical Characterization.
- Authors
Mnif, Ibtissem; Siala, Rayda; Nasri, Rim; Mhamdi, Samiha; Nasri, Moncef; Kamoun, Alya
- Abstract
A plant protease named microcarpain was purified from the latex of Ficus microcarpa by acetonic (20-40 % saturation) precipitation, Sephadex G-75 filtration, and Mono Q-Sefinose FF chromatography. The protease was purified with a yield of 9.25 % and a purification factor of 8. The molecular weight of the microcarpain was estimated to be 20 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The purified enzyme showed maximum activity at pH 8.0 and at a temperature of 70 °C. Proteolytic activity was strongly inhibited by dithio-bis-nitrobenzoic acid (DTNB), Hg, and Cu. The N-terminal amino acid sequence of the purified microcarpain 'VPETVDWRSKGAV' showed high homology with a protease from Arabidopsis thaliana. Inhibition studies and N-terminal sequence classified the enzyme as a member of the cysteine peptidases family.
- Subjects
CYSTEINE proteinases; LATEX; FICUS (Plants); BOTANICAL chemistry; CHEMICAL purification; POLYACRYLAMIDE gel electrophoresis; SEPHADEX; NITROBENZOIC acid
- Publication
Applied Biochemistry & Biotechnology, 2015, Vol 175, Issue 3, p1732
- ISSN
0273-2289
- Publication type
Article
- DOI
10.1007/s12010-014-1376-2