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Purification, crystallization and preliminary X‐ray analysis of CMS1MS2: a cysteine proteinase from Carica candamarcensis latex

Purification, crystallization and preliminary X‐ray analysis of CMS1MS2: a cysteine proteinase... Cysteine proteinases from the latex of plants of the family Caricaceae are widely used industrially as well as in pharmaceutical preparations. In the present work, a 23 kDa cysteine proteinase from Carica candamarcensis latex (designated CMS1MS2) was purified for crystallization using three chromatography steps. The enzyme shows about fourfold higher activity than papain with BAPNA as substrate. Crystals suitable for X‐ray diffraction experiments were obtained by the hanging‐drop method in the presence of PEG and ammonium sulfate as precipitants. The crystals are monoclinic (space group P21), with unit‐cell parameters a = 53.26, b = 75.71, c = 53.23 Å, β = 96.81°, and diffract X‐rays to 1.8 Å resolution. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

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References (2)

Publisher
Wiley
Copyright
International Union of Crystallography, 2008
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S174430910801172X
pmid
18540057
Publisher site
See Article on Publisher Site

Abstract

Cysteine proteinases from the latex of plants of the family Caricaceae are widely used industrially as well as in pharmaceutical preparations. In the present work, a 23 kDa cysteine proteinase from Carica candamarcensis latex (designated CMS1MS2) was purified for crystallization using three chromatography steps. The enzyme shows about fourfold higher activity than papain with BAPNA as substrate. Crystals suitable for X‐ray diffraction experiments were obtained by the hanging‐drop method in the presence of PEG and ammonium sulfate as precipitants. The crystals are monoclinic (space group P21), with unit‐cell parameters a = 53.26, b = 75.71, c = 53.23 Å, β = 96.81°, and diffract X‐rays to 1.8 Å resolution.

Journal

Acta Crystallographica Section FWiley

Published: Jun 1, 2008

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