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2004 | 51 | 1 | 213-218
Article title

AMP-deaminase from hen stomach smooth muscle - physico-chemical properties of the enzyme.

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EN
Abstracts
EN
AMP-deaminase from hen stomach smooth muscle was isolated and physico-chemical properties of the purified enzyme were investigated. The enzyme had an activity optimum at pH 6.5, and poorly deaminated the substrate analogues tested. At optimum pH (6.5), in the absence of regulatory ligands (control conditions), the enzyme manifested hyperbolic substrate-saturation kinetics with half-saturation constant (S0.5) of about 4.5 mM. Additions of adenine nucleotide effectors (ATP, ADP) activated the enzyme strongly at all the concentrations tested, diminishing significantly the value of S0.5 constant. In contrast, the regulatory effect of orthophosphate was variable, and depended on the orthophosphate concentration used. The molecular mass of the enzyme subunit determined in SDS/PAG electrophoresis was about of 37 kDa. The obtained results suggest that in different types of hen muscle, similarly as in humans and rats, expression of AMP-deaminase is under the control of independent genes.
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Publisher

Year
Volume
51
Issue
1
Pages
213-218
Physical description
Dates
published
2004
received
2003-07-23
revised
2004-01-20
accepted
2004-02-06
Contributors
author
  • Department of Biochemistry, Medical University of Gdansk, Gdańsk, Poland
  • Department of Biochemistry, Medical University of Gdansk, Gdańsk, Poland
author
  • Department of Pharmaceutical Biochemistry, Medical University of Gdansk, Gdańsk, Poland
author
  • Department of Pharmaceutical Biochemistry, Medical University of Gdansk, Gdańsk, Poland
  • Department of Biochemistry, Medical University of Gdansk, Gdańsk, Poland
References
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Document Type
Publication order reference
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YADDA identifier
bwmeta1.element.bwnjournal-article-abpv51i1p213kz
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