Cited by 153Cynara cardunculus studiesPineapple and bromelain studiesEnzyme Production and Characterization

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Purification, Characterization and Partial Amino Acid Sequencing of Two New Aspartic Proteinases from Fresh Flowers of Cynara cardunculus L.

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Veríssimo, Paula, Faro, Carlos, Moir, Arthur J. G., Lin, Yingzhang, Tang, Jordan, Pires, Euclides·1996·European Journal of Biochemistry

DOI 10.1111/j.1432-1033.1996.00762.x

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Abstract

Two new aspartic proteinases have been isolated from stigmas of the cardoon Cynara cardunculus L. by a two‐step purification procedure including extraction at low pH, gel filtration on Superdex 200, and ion‐exchange chromatography on Mono Q. To follow the conventional nomenclature for aspartic proteinases, we have named these proteinases cardosin A and cardosin B. On SDS/PAGE, cardosin A migrated as two bands with apparent molecular masses of 31 000 Da and 15000 Da where as the chains of cardosin B migrated as bands of 34000 Da and 14000 Da. The partial amino acid sequences of the two cardosins revealed that they are similar but not identical, and that they differ horn the previously reported cardoon proteinases named cynarases, which were assumed to be derived from a common precursor. Although the cardosins show some degree of similarity to each other, we could detect no immunological cross‐reactivity between them. Both cardosins were active at low pH and were inhibited by pepstatin, with Ki values of 3 nM for cardosin A and 1 nM for cardosin B, indicating that they belong to the class of aspartic proteinases. Significant differences between the two enzymes were also found for the Kcat/Km values for the hydrolysis of two chromophoric synthetic peptides. The active‐site ionization constants, pK e1 and pK e2, for cardosin A are 2.5±0.2 and 5.3±20.2, whereas for cardosin R they are 3.73±10.09 and 6.7±50.1. The results herein described on the structural and kinetic properties of the cardosins indicate that they are the products of distinct genes which have probably arisen by gene duplication. A scheme for the proteolytic processing of the two enzymes is also proposed.

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Authors: Veríssimo, P., Faro, C., Moir, A. J. G., Lin, Y., Tang, J., & Pires, E.
Affiliations: University of Coimbra (PT)
University of Sheffield (GB)
Oklahoma Medical Research Foundation (US)
Corresponding author: Faro, Carlos
ORCID: Faro, Carlos
Pires, Euclides
Venue: European Journal of Biochemistry
Publisher: Wiley
Published: 1996-02
Volume: 235
Issue: 3
Pages: 762-768
ISSN: 0014-2956 (ISSN-L)
1432-1033
DOI: 10.1111/j.1432-1033.1996.00762.x
OpenAlex: W2086022519
Semantic Scholar: 7a83370164b5faf18b9386004bed408419f09581
Cited by: 153
References: 39
Citations by year: 2026: 1 · 2025: 2 · 2024: 1 · 2023: 4 · 2022: 6 · 2021: 2 · 2020: 11 · 2019: 2 · 2018: 6 · 2017: 5 · 2016: 3 · 2015: 4 · 2014: 2 · 2013: 5 · 2012: 4
FWCI: 12.12
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor, 3134 d)
Locations: European Journal of Biochemistry (publishedVersion)
PubMed (publishedVersion)
Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) (submittedVersion, other-oa)
Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) (submittedVersion)
Topics: Life Sciences › Agricultural and Biological Sciences › Plant Science › Cynara cardunculus studies
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Pineapple and bromelain studies
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
Keywords: aspartic protease, Cynara cardunculus, stigma (botany), enzyme purification, partial amino acid sequence, pepstatin inhibition, enzyme kinetics, gene duplication, proteolytic processing, immunological cross-reactivity
MeSH terms: Amino Acid Sequence, Chromatography, Gel, Chromatography, High Pressure Liquid, Electrophoresis, Polyacrylamide Gel, Hydrogen-Ion Concentration, Kinetics, Molecular Sequence Data, Plant Proteins, Plants, Protein Processing, Post-Translational, Blotting, Western, Aspartic Acid Endopeptidases, Sequence Alignment

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Purification, Characterization and Partial Amino Acid Sequencing of Two New Aspartic Proteinases from Fresh Flowers of Cynara cardunculus L.

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