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Purification and characterisation of adenosine nucleosidase from Coffea arabica young leaves

Title
Purification and characterisation of adenosine nucleosidase from Coffea arabica young leaves
Type
Article in International Scientific Journal
Year
2005
Authors
Alexandre Campos
(Author)
Other
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Rijo Johansen, MJ
(Author)
Other
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Fevereiro, P
(Author)
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Journal
Title: PhytochemistryImported from Authenticus Search for Journal Publications
Vol. 66
Pages: 147-151
ISSN: 0031-9422
Publisher: Elsevier
Other information
Authenticus ID: P-000-6FQ
Abstract (EN): An adenosine nucleosidase (ANase) (EC 3.2.2.7) was purified from young leaves of Coffea arabica L. cv. Catimor. A sequence of fractionating steps was used starting with ammonium sulphate salting-out, followed by anion exchange, hydrophobic interaction and gel filtration chromatography. The enzyme was purified 5804-fold and a specific activity of 8333 nkatmg(-1) protein was measured. The native enzyme is a homodimer with an apparent molecular weight of 72 kDa estimated by gel filtration and each monomer has a molecular weight of 34.6 kDa, estimated by SDS-PAGE. The enzyme showed maximum activity at pH 6.0 in citrate-phosphate buffer (50 mM). The calculated K-m is 6.3 muM and V-max 9.8 nKat.
Language: English
Type (Professor's evaluation): Scientific
No. of pages: 5
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