ArticleJournal of protein chemistry2001
Two new cysteine endopeptidases obtained from the latex of Araujia hortorum fruits.
Article in Journal of protein chemistry, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 45 citations in OpenAlex.
- Production of Plant Proteases and New Biotechnological Applications: An Updated Review.ChemistryOpen · 2022Review
- 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 characterization of a new plant endopeptidase isolated from latex of Asclepias fruticosa L. (Asclepiadaceae).Journal of protein chemistry · 2001Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two new endopeptidases were purified to homogeneity from the latex of Araujia hortorum fruits by a simple purification procedure involving ultracentrifugation and ion exchange chromatography. Molecular weights of araujiain h II and araujiain h III were 23,718 and 23546 (mass spectrometry), respectively. The isoelectric point of araujiain h II was 8.9, whereas araujiain h III had a pI higher than 9.3. Maximum proteolytic activity on caseine was reached at pH 8.0-9.0 for both endopeptidases, which were irreversibly inhibited by iodoacetate and E-64, suggesting they belong to the cysteine protease family. Esterolytic activity was determined on N-alpha-CBZ-amino acid-p-nitrophenyl esters, and the highest kcat/Km values for the both enzymes were obtained with the glutamine derivative. The N-terminal sequences of araujiain h II and araujiain h III showed a high degree of homology with other plant cysteine endopeptidases.
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