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

• Authors: Anna Swieca , Iwona Rybakowska , Anna Koryziak , Jerzy Klimek , Krystian Kaletha
• Languages of publication: 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.

Keywords

EN

AMP-deaminase; smooth muscle

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2004
• Volume: 51
• Issue: 1
• Pages: 213-218

Dates

published

2004

received

2003-07-23

revised

2004-01-20

accepted

2004-02-06

Contributors

author

Anna Swieca

• Department of Biochemistry, Medical University of Gdansk, Gdańsk, Poland

author

Iwona Rybakowska

• Department of Biochemistry, Medical University of Gdansk, Gdańsk, Poland

author

Anna Koryziak

• Department of Pharmaceutical Biochemistry, Medical University of Gdansk, Gdańsk, Poland

author

Jerzy Klimek

• Department of Pharmaceutical Biochemistry, Medical University of Gdansk, Gdańsk, Poland

author

Krystian Kaletha

• Department of Biochemistry, Medical University of Gdansk, Gdańsk, Poland

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