Purification and properties of acid phosphatase (EC 3.1.3.2) secreted by strain 74A of the mould Neurospora crassa
Carregando...
Arquivos
Fontes externas
Fontes externas
Data
Autores
Orientador
Coorientador
Pós-graduação
Curso de graduação
Título da Revista
ISSN da Revista
Título de Volume
Editor
Rapid Science Publishers
Tipo
Artigo
Direito de acesso
Acesso restrito
Arquivos
Fontes externas
Fontes externas
Resumo
Both P-i-repressible acid phosphatases, IIb (mycelial) and IIc (extracellular), synthesized by Neurospora crassa and purified to apparent homogeneity by 7.5% PAGE, are monomers, are inhibited by 2 mM ZnCl2 and are nonspecifically stimulated by salts. However, the IIc form is activated by p-nitrophenylphosphate (in a negative cooperativity effect with a K-0.5 of 2.5 mM) whereas form IIb shows Michaelis kinetics, with a K-m of 0.5 mM. Thus, since both enzymatic forms may be expressed by the same gene (pho-3), it is possible that post-translational modifications lead to the excretion of an enzymatic form with altered Michaelis kinetics compared with the enzymatic form retained by the mycelium.
Descrição
Palavras-chave
acid phosphatase, enzyme secretion, fungi, Neurospora crassa, phosphate regulation
Idioma
Inglês
Citação
World Journal of Microbiology & Biotechnology. London: Rapid Science Publishers, v. 12, n. 1, p. 109-110, 1996.
