ArticleJournal of protein chemistry2000
Isolation and characterization of a cysteine protease from the latex of Araujia hortorum fruits.
Article in Journal of protein chemistry, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 76 citations in OpenAlex.
- Production of Plant Proteases and New Biotechnological Applications: An Updated Review.ChemistryOpen · 2022Review
- Characterization of thermo- and detergent stable antigenic glycosylated cysteine protease of Euphorbia nivulia Buch.-Ham. and evaluation of its ecofriendly applications.TheScientificWorldJournal · 2013Article
- Article
- Philibertain g I, the most basic cysteine endopeptidase purified from the latex of Philibertia gilliesii Hook. et Arn. (Apocynaceae).The protein journal · 2005Article
- Purification and biochemical characterization of asclepain c I from the latex of Asclepias curassavica L.The protein journal · 2004Article
- Funastrain c II: a cysteine endopeptidase purified from the latex of Funastrum clausum.The protein journal · 2004Article
- Morrenain b I, a papain-like endopeptidase from the latex of Morrenia brachystephana Griseb. (Asclepiadaceae).Journal of protein chemistry · 2003Article
- Purification and biochemical characterization of a highly active cysteine protease ervatamin A from the latex of Ervatamia coronaria.Journal of protein chemistry · 2003Article
- Purification and characterization of a new plant endopeptidase isolated from latex of Asclepias fruticosa L. (Asclepiadaceae).Journal of protein chemistry · 2001Article
- Two new cysteine endopeptidases obtained from the latex of Araujia hortorum fruits.Journal of protein chemistry · 2001Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A new protease (araujiain h I) was purified to mass spectroscopy homogeneity from the latex of Araujia hortorum Fourn. (Asclepiadaceae) fruits by ultracentrifugation and ion exchange chromatography. The enzyme has a molecular mass of 24,031 (mass spectrometry) and an iso-electric point higher than 9.3. The optimum pH range for casein hydrolysis was 8.0-9.5. The enzyme showed remarkable caseinolytic activity at high temperatures, although its thermal stability decayed rapidly. The proteinase was activated by thiol compounds and inhibited by common thiol-blocking reagents, particularly E-64 and HgCl2, suggesting the enzyme belongs to the cysteine protease family. The concentration of active sites as determined by titration with E-64 was 3.3 microM. When assayed on N-alpha-CBZ-amino acid-p-nitrophenyl esters, the enzyme showed higher preference for the glutamine derivative, followed by those of alanine, asparagine, glycine, and leucine, in decreasing order. Partial homology (36-48%) with other plant cysteine proteinases was observed in an internal fragment obtained by Protease V8 treatment.
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