Carboxypeptidase
Mostrando 1-12 de 505 artigos, teses e dissertações.
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1. Changes in digestive enzymes activities during the initial ontogeny of wolf cichlid, Parachromis dovii (Perciformes: Cichlidae)
ABSTRACT Wolf cichlid, Parachromis dovii, is a species with a high potential for aquaculture in Central America; however, the knowledge of the digestive physiology in larvae period is limited. For these reason, this study evaluated the changes on digestive enzymes (alkaline and acid proteases, trypsin, chymotrypsin, aminopeptidase, carboxypeptidase, lipases,
Neotrop. ichthyol.. Publicado em: 29/04/2019
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2. Partial characterization of digestive proteases in sheepshead, Archosargus probatocephalus (Spariformes: Sparidae)
ABSTRACT Digestive proteases were partially characterized in sheepshead juveniles, using biochemical and electrophoretic techniques. Results showed higher activity level of the stomach proteases (2.39 ± 0.02 U mg protein-1) compared to the intestinal proteases (1.6 ± 0.1 U mg protein-1). The activity of trypsin, chymotrypsin, leucine aminopeptidase and car
Neotrop. ichthyol.. Publicado em: 08/11/2018
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3. Protease prospecion and determination of its isoenzymes activity in cocoa cultivars (Theobroma cacao L.)
Abstract Our objective was to characterize the protease enzymatic activity and its isoenzymes on cacao cultivars PH 16 and TSH 1188, produced in southern Bahia, linking it to the conditions of the fermentation process. Proteases were extracted and semi-purified, their activities determined changing substrate, pH and temperature, and the values compared with
Food Sci. Technol. Publicado em: 13/04/2017
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4. Enzymatic activity of proteases and its isoenzymes in fermentation process in cultivars of cocoa (Theobroma cacao L.) produced in southern Bahia, Brazil
Abstract The fermentation of cocoa seeds envolves microbial processes and the action of enzymes. To identify the possible differences in the cocoa fermentation process, with regards to proteolysis, this study has the objective of determining protease activity (under predetermined conditions) and its isoenzymes in two cocoa cultivars (PH-16 and HRT-1188) in d
Food Sci. Technol. Publicado em: 21/11/2016
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5. Investigação da Carboxipeptidase, Esfingomielinase e Fosfatase Alcalina de Schistosoma mansoni como potenciais antígenos. / Investigation of Carboxypeptidase, Sphingomyelinase and Alkaline Phosphatase from Schistosoma mansoni as potential vaccine candidates.
A esquistossomose representa um grande problema de saúde pública em regiões tropicais, negligenciado pelas empresas farmacêuticas. Três genes foram selecionados a partir do transcriptoma do S. mansoni para serem caracterizados molecularmente e testados como vacinas. O gene da Carboxipeptidase apresentou altos níveis de transcrição no estágio de cerc
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 20/10/2011
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6. ECA e receptor AT1 participam da mecanotransdução de sinais hemodinâmicos independentemente da angiotensina II / ACE and AT1 receptor are involved in mechanotransduction by hemodynamica forces independently of angiotensin II
Hemodynamic forces such as pressure and shear stress modulate the patophysiolgy of the cardiovascular system. In this study, we investigated two transmembranic key molecules of the renin-angiotensin system (RAS) as mechanosensors and mechanotransducers of physical forces: Angiotensin Converting Enzyme (ACE) and Angiotensin II type 1 Receptor (AT1). ACE is an
Publicado em: 2010
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7. Purification and characterization of a carboxypeptidase and a dipeptidase from Tenebrio molitor (Coleoptera) larvae / Purificação e caracterização de uma carboxipeptidase e de uma dipeptidase da larva de Tenebrio molitor (Coleoptera)
Devido aos problemas, ambientais e à população humana, causados pelos inseticidas químicos, novas investigações para o controle de insetos tornaram-se necessárias. Para isto, um maior conhecimento sobre a fisiologia digestiva dos insetos torna-se essencial, visto que o intestino é uma interface, grande e relativamente desprotegida, entre o inseto e o
Publicado em: 2008
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8. High expression of human carboxypeptidase M in Pichia pastoris: Purification and partial characterization
Carboxypeptidase M (CPM) is an extracellular glycosylphosphatidyl-inositol-anchored membrane glycoprotein, which removes the C-terminal basic residues, lysine and arginine, from peptides and proteins at neutral pH. CPM plays an important role in the control of peptide hormones and growth factor activity on the cell surface. The present study was carried out
Brazilian Journal of Medical and Biological Research. Publicado em: 2006-02
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9. Human mast cell carboxypeptidase. Purification and characterization.
A carboxypeptidase activity was recently identified in highly purified human lung mast cells and dispersed mast cells from skin. Using affinity chromatography with potato-tuber carboxypeptidase inhibitor as ligand, mast cell carboxypeptidase was purified to homogeneity from whole skin extracts. The purified enzyme yielded a single staining band of approximat
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10. Carboxypeptidase B-like converting enzyme activity in secretory granules of rat pituitary.
Recent amino acid sequence data suggest that trypsin-like and carboxypeptidase B-like activities are required for the processing of pituitary prohormones--e.g., pro-opiocortin (pro-adrenocorticotropin/lipotropin) and provasopressin in secretory granules. In this study the existence of a carboxypeptidase B activity in purified secretory granules from anterior
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11. Amino-acid sequence of bovine carboxypeptidase B.
The amino-acid sequence of bovine carboxypeptidase B [peptidyl-L-lysine(-L-arginine)hydrolase, EC 3.4.12.3] has been determined using the heavy and light chains of the enzyme isolated from spontaneously activated pancreatic juice. Comparison of the sequence with that of carboxypeptidase A shows that the two enzymes are homologous (49% identity) and that all
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12. Tomato Fruit Carboxypeptidase (Properties, Induction upon Wounding, and Immunocytochemical Localization).
Carboxypeptidase activity was characterized during ripening and wounding of tomato (Lycopersicon esculentum) fruit. The fruit enzyme shares substrate specificity and susceptibility to the inhibitors diisopropyl fluorophosphate and phenylmethylsulfonyl fluoride with other plant carboxypeptidases. The abundance and stability of wound-induced carboxypeptidase w