Purification and characterization of an inorganic pyrophosphatase from the extreme thermophile Thermus aquaticus.

An inorganic pyrophosphatase was purified over 600-fold to homogeneity as judged by polyacrylamide gel electrophoresis. The enzyme is a tetramer of Mr = 84,000, has a sedimentation coefficient of 5.8S, a Stokes radius of 3.5 nm, and an isoelectric point of 5.7. Like the enzyme of Escherichia coli, t...

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Detaylı Bibliyografya
Asıl Yazarlar: Verhoeven, J A, Schenck, K M, Meyer, R R, Trela, J M
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: 1986
Konular:
Research Article
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC213453/
https://ncbi.nlm.nih.gov/pubmed/3020000
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