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Purification and properties of methylamine dehydrogenase from Paracoccus denitrificans.

Methylamine dehydrogenase from Paracoccus denitrificans was purified to homogeneity in two steps from the periplasmic fraction of methylamine-grown cells. The enzyme exhibited a pI value of 4.3 and was composed of two 46,700-dalton subunits and two 15,500-dalton subunits. Each small subunit possesse...

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Detalles Bibliográficos
Publicado en:J Bacteriol
Principais autores: Husain, M, Davidson, V L
Formato: Artigo
Idioma:Inglês
Publicado: American Society for Microbiology (ASM) 1987
Assuntos:
Acceso en liña:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC212003/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/3558322/
https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.169.4.1712-1717.1987
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