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

100%

Swieca A., Rybakowska I., Koryziak A., Klimek J., Kaletha K.

Acta Biochimica Polonica

2004

tom 51

nr 1

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 GS0.5) 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.

Properties of AMP-deaminase in ontogenesis of human hearts

86%

Rybakowska I., Swiatkowska-Freund M., Emerich J., Kortecka M., Krzyzanowski M., Kaletha K.

Acta Biochimica Polonica

2003

tom 50

nr Supplement 1

Ograniczanie wyników

2 Acta Biochimica Polonica

2 Kaletha K.

2 Rybakowska I.

1 Emerich J.

1 Klimek J.

1 Kortecka M.

1 Koryziak A.

1 Krzyzanowski M.

1 Swiatkowska-Freund M.

1 Swieca A.

1 2004

1 2003

Wyniki wyszukiwania

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

Properties of AMP-deaminase in ontogenesis of human hearts