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	Provedor de dados BJMBR (2) Autor Chagas,J.R. (2) Almeida,P.C. (1) Araújo,R.C. (1) Casarini,D.E. (1) Craveiro,R.B. (1) Pesquero,J.B. (1) Pesquero,J.L. (1) Pimenta,D.C. (1) Ramalho,J.D. (1) Tersariol,I.L.S. (1) Wang,P.H.M. (1) Mais... Palavra-chave Glycosaminoglycan (1) Heparin binding (1) Human carboxypeptidase M (1) Kinins (1) Macromolecules (1) Pichia pastoris (1) Proteinases (1) Recombinant protein (1) Mais... Tipo do documento Info:eu-repo/semantics/article (2) Ano 2006 (1) 2002 (1) País Brazil (2) Idioma Inglês (2)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 2 Primeira ... 1 ... Última High expression of human carboxypeptidase M in Pichia pastoris: Purification and partial characterization BJMBR Craveiro,R.B.; Ramalho,J.D.; Chagas,J.R.; Wang,P.H.M.; Casarini,D.E.; Pesquero,J.L.; Araújo,R.C.; Pesquero,J.B.. 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 to clone and express human CPM in the yeast Pichia pastoris in order to evaluate the importance of this enzyme in physiological and pathological processes. The cDNA for the enzyme was amplified from total placental RNA by RT-PCR and cloned in the vector pPIC9, which uses the methanol oxidase promoter and drives the expression of high levels of heterologous proteins in P. pastoris. The cpm gene, after... Tipo: Info:eu-repo/semantics/article Palavras-chave: Kinins; Human carboxypeptidase M; Recombinant protein; Pichia pastoris. Ano: 2006 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2006000200007 Proteinase activity regulation by glycosaminoglycans BJMBR Tersariol,I.L.S.; Pimenta,D.C.; Chagas,J.R.; Almeida,P.C.. There are few reports concerning the biological role and the mechanisms of interaction between proteinases and carbohydrates other than those involved in clotting. It has been shown that the interplay of enzymes and glycosaminoglycans is able to modulate the activity of different proteases and also to affect their structures. From the large number of proteases belonging to the well-known protease families and also the variety of carbohydrates described as widely distributed, only few events have been analyzed more deeply. The term "family" is used to describe a group of proteases in which every member shows an evolutionary relationship to at least one other protease. This relationship may be evident throughout the entire sequence, or at least in that part... Tipo: Info:eu-repo/semantics/article Palavras-chave: Proteinases; Heparin binding; Glycosaminoglycan; Macromolecules. Ano: 2002 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2002000200001 Registros recuperados: 2 Primeira ... 1 ... Última

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