Purification and partial characterization of cathepsin D from porcine (Sus scrofa) liver using affinity chromatography
Carregando...
Fonte externa
Fonte externa
Data
Orientador
Coorientador
Pós-graduação
Curso de graduação
Título da Revista
ISSN da Revista
Título de Volume
Editor
Academic Press Aust
Tipo
Artigo
Direito de acesso
Acesso aberto
Fonte externa
Fonte externa
Resumo
Cathepsin D, a lysosomal aspartic protease, has been purified from porcine liver using a combination of pepstatin-A agarose and Affi-Gel Blue affinity chromatography, followed by size-exclusion chromatography. The purified protein consists of two polypeptide chains of 15 and 30 kDa, and has an isoelectric point of 6.8. Porcine liver cathepsin D has maximum activity at pH 2.5-3.0 as determined by its activity against hemoglobin, with a K-cat of 14.3 s(-1) and a k(cat)/K-M of 2.70 x 10(6) s(-1) M-1 as determined by the hydrolysis of a fluorogenic peptide substrate.
Descrição
Palavras-chave
cathepsin D, aspartic protease, lysosomal enzyme, affinity chromatography, pepstatin A
Idioma
Inglês
Citação
Biochemistry and Molecular Biology International. Marrickville: Academic Press Aust, v. 45, n. 4, p. 797-803, 1998.
