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Multiplicity of aspartic proteinases from Cynara cardunculus L.

(2009) PLANTA. 230(2). p.429-439
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Organization
Abstract
Aspartic proteinases (AP) play major roles in physiologic and pathologic scenarios in a wide range of organisms from vertebrates to plants or viruses. The present work deals with the purification and characterisation of four new APs from the cardoon Cynara cardunculus L., bringing the number of APs that have been isolated, purified and biochemically characterised from this organism to nine. This is, to our knowledge, one of the highest number of APs purified from a single organism, consistent with a specific and important biological function of these protein within C. cardunculus. These enzymes, cardosins E, F, G and H, are dimeric, glycosylated, pepstatin-sensitive APs, active at acidic pH, with a maximum activity around pH 4.3. Their primary structures were partially determined by N- and C-terminal sequence analysis, peptide mass fingerprint analysis on a MALDI-TOF/TOF instrument and by LC-MS/MS analysis on a Q-TRAP instrument. All four enzymes are present on C. cardunculus L. pistils, along with cyprosins and cardosins A and B. Their micro-heterogeneity was detected by 2D-electrophoresis and mass spectrometry. The enzymes resemble cardosin A more than they resemble cardosin B or cyprosin, with cardosin E and cardosin G being more active than cardosin A, towards the synthetic peptide KPAEFF(NO2)AL. The specificity of these enzymes was investigated and it is shown that cardosin E, although closely related to cardosin A, exhibits different specificity.
Keywords
SEQUENCE-ANALYSIS, EXPRESSION, SPECIFICITY, PROTEASE, CHYMOSIN, PURIFICATION, FLOWERS, Protein characterisation, Specificity, Mass spectrometry, Aspartic proteinases, RECOMBINANT CYPROSIN, ORGANIC-SOLVENTS, CARDOSIN-A

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Citation

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MLA
Sarmento, Ana Cristina et al. “Multiplicity of Aspartic Proteinases from Cynara Cardunculus L.” PLANTA 230.2 (2009): 429–439. Print.
APA
Sarmento, A. C., Lopes, H., Oliveira, C. S., Vitorino, R., Samyn, B., Sergeant, K., Debyser, G., et al. (2009). Multiplicity of aspartic proteinases from Cynara cardunculus L. PLANTA, 230(2), 429–439.
Chicago author-date
Sarmento, Ana Cristina, Henrique Lopes, Claudia S Oliveira, Rui Vitorino, Bart Samyn, Kjell Sergeant, Griet Debyser, et al. 2009. “Multiplicity of Aspartic Proteinases from Cynara Cardunculus L.” Planta 230 (2): 429–439.
Chicago author-date (all authors)
Sarmento, Ana Cristina, Henrique Lopes, Claudia S Oliveira, Rui Vitorino, Bart Samyn, Kjell Sergeant, Griet Debyser, Jozef Van Beeumen, Pedro Domingues, Francisco Amado, Euclides Pires, M Rosario M Domingues, and Marlene T Barros. 2009. “Multiplicity of Aspartic Proteinases from Cynara Cardunculus L.” Planta 230 (2): 429–439.
Vancouver
1.
Sarmento AC, Lopes H, Oliveira CS, Vitorino R, Samyn B, Sergeant K, et al. Multiplicity of aspartic proteinases from Cynara cardunculus L. PLANTA. 2009;230(2):429–39.
IEEE
[1]
A. C. Sarmento et al., “Multiplicity of aspartic proteinases from Cynara cardunculus L.,” PLANTA, vol. 230, no. 2, pp. 429–439, 2009.
@article{956993,
  abstract     = {Aspartic proteinases (AP) play major roles in physiologic and pathologic scenarios in a wide range of organisms from vertebrates to plants or viruses. The present work deals with the purification and characterisation of four new APs from the cardoon Cynara cardunculus L., bringing the number of APs that have been isolated, purified and biochemically characterised from this organism to nine. This is, to our knowledge, one of the highest number of APs purified from a single organism, consistent with a specific and important biological function of these protein within C. cardunculus. These enzymes, cardosins E, F, G and H, are dimeric, glycosylated, pepstatin-sensitive APs, active at acidic pH, with a maximum activity around pH 4.3. Their primary structures were partially determined by N- and C-terminal sequence analysis, peptide mass fingerprint analysis on a MALDI-TOF/TOF instrument and by LC-MS/MS analysis on a Q-TRAP instrument. All four enzymes are present on C. cardunculus L. pistils, along with cyprosins and cardosins A and B. Their micro-heterogeneity was detected by 2D-electrophoresis and mass spectrometry. The enzymes resemble cardosin A more than they resemble cardosin B or cyprosin, with cardosin E and cardosin G being more active than cardosin A, towards the synthetic peptide KPAEFF(NO2)AL. The specificity of these enzymes was investigated and it is shown that cardosin E, although closely related to cardosin A, exhibits different specificity.},
  author       = {Sarmento, Ana Cristina and Lopes, Henrique and Oliveira, Claudia S and Vitorino, Rui and Samyn, Bart and Sergeant, Kjell and Debyser, Griet and Van Beeumen, Jozef and Domingues, Pedro and Amado, Francisco and Pires, Euclides and Domingues, M Rosario M and Barros, Marlene T},
  issn         = {0032-0935},
  journal      = {PLANTA},
  keywords     = {SEQUENCE-ANALYSIS,EXPRESSION,SPECIFICITY,PROTEASE,CHYMOSIN,PURIFICATION,FLOWERS,Protein characterisation,Specificity,Mass spectrometry,Aspartic proteinases,RECOMBINANT CYPROSIN,ORGANIC-SOLVENTS,CARDOSIN-A},
  language     = {eng},
  number       = {2},
  pages        = {429--439},
  title        = {Multiplicity of aspartic proteinases from Cynara cardunculus L.},
  url          = {http://dx.doi.org/10.1007/s00425-009-0948-9},
  volume       = {230},
  year         = {2009},
}

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