Encontrados 5 documentos, a visualizar página 1 de 1
Crystal structure of a novel cysteinless plant Kunitz-type protease inhibitor
Hansen, Daiane; Macedo-Ribeiro, Sandra; Veríssimo, Paula; Yoo Im, Sonia; Sampaio, Misako Uemura; Oliva, Maria Luiza VilelaBauhinia bauhinioides Cruzipain Inhibitor (BbCI) is a cysteine protease inhibitor highly homologous to plant Kunitz-type inhibitors. However, in contrast to classical Kunitz family inhibitors it lacks cysteine residues and therefore disulfide bridges. BbCI is also distinct in the ability to inactivate enzymes belonging to two different classes, cysteine and serine proteases. Besides inhibiting the cysteine prot...
Molecular cloning and characterization of cDNA encoding cardosin B, an aspartic...
Vieira, Margarida; Pissarra, José; Veríssimo, Paula; Castanheira, Pedro; Costa, Yael; Pires, Euclides; Faro, CarlosCardosins A and B are related aspartic proteinases from the pistils of Cynara cardunculus L., whose milk-clotting activity has been exploited for the manufacture of cheese. Here we report the cloning of cardosin B cDNA and its organ, tissue and cytological localization. The cDNA-derived amino acid sequence has 73% similarity with that of cardosin A and displays several distinguishing features. Cardosin B mRNA w...
Identification and proteolytic processing of procardosin A
Ramalho-Santos, Miguel; Veríssimo, Paula; Cortes, Luísa; Samyn, Bart; Beeumen, Jozef Van; Pires, Euclides; Faro, CarlosPlant aspartic proteinases contain a plant-specific insert (PSI) of about 100 amino acids of unknown function with no similarity with the other aspartic proteinases but with significant similarity with saposins, animal sphingolipid activator proteins. PSI has remained elusive at the protein level, suggesting that it may be removed during processing. To understand the molecular relevance of PSI, the proteolytic ...
The Glycosylation of the Aspartic Proteinases from Barley (Hordeum Vulgare L.) ...
Costa, Júlia; Ashford, David A.; Nimtz, Manfred; Bento, Isabel; Frazão, Carlos; Esteves, Cristina L.; Faro, Carlos J.; Kervinen, Jukka; Pires, EuclidesPlant aspartic proteinases characterised at the molecular level contain one or more consensus N-glycosylation sites [Runeberg-Roos, P., Törmäkangas, K. & Östman, A. (1991) Eur. J. Biochem. 202, 102120131027; Asakura, T., Watanabe, H., Abe, K. & Arai, S. (1995) Eur. J. Biochem. 232, 77201383; Veríssimo, P., Faro, C., Moir, A. J. G., Lin, Y., Tang, J. & Pires, E. (1996) Eur. J. Biochem. 235, 76220137681. We found...
Purification, Characterization and Partial Amino Acid Sequencing of Two New Asp...
Veríssimo, Paula; Faro, Carlos; Moir, Arthur J. G.; Lin, Yingzhang; Tang, Jordan; Pires, EuclidesTwo 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 w...
| Financiadores do RCAAP | |||||||
|
|
|
|
|
|
||