ArticleThe protein journal2008
Purification and characterization of four new cysteine endopeptidases from fruits of Bromelia pinguin L. grown in Cuba.
Article in The protein journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 31 citations in OpenAlex.
- Peptidases from Maclura Pomifera for Preparation of Food Protein Hydrolysates: Purification by Single-Step Chromatography and Characterization of Pomiferin I.Applied biochemistry and biotechnology · 2021Article
- Enzyme activity and partial characterization of proteases obtained fromFood science and biotechnology · 2018Article
- Article
- Penduliflorain I: A cysteine protease isolated from Hohenbergia penduliflora (A.Rich.) Mez (Bromeliaceae).The protein journal · 2010Article
- Physicochemical, nutritional and antibacterial characteristics of the fruit of Bromelia pinguin L.Plant foods for human nutrition (Dordrecht, Netherlands) · 2009Article
- Purification and characterization of hieronymain III. Comparison with other proteases previously isolated from Bromelia hieronymi Mez.The protein journal · 2008Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bromelia pinguin L. is a plant broadly distributed in Central America and Caribbean islands. The fruits have been used in traditional medicine as anthelmintic, probably owed to the presence of a mixture of cysteine endopeptidases, initially termed pinguinain. This work deals with the purification and characterization of the four main components of that mixture, two of them showing acid pI and the other two alkaline pI. Molecular masses (SDS-PAGE and MALDI-TOF), N-terminal sequence and the reactivity and kinetic parameters versus synthetic substrates (p-nitrophenyl-N-alpha-CBZ-amino acid esters, PFLNA, Z-Arg-Arg-p-NA, and Z-Phe-Arg-p-NA) of the studied peptidases are given, as well as the N-terminal sequences of the enzymes and the homology degree with other plant endopeptidases.
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