- Tytuł:
- AMP-deaminase from hen stomach smooth muscle - physico-chemical properties of the enzyme.
- Autorzy:
-
Swieca, Anna
Rybakowska, Iwona
Koryziak, Anna
Klimek, Jerzy
Kaletha, Krystian - Powiązania:
- https://bibliotekanauki.pl/articles/1043348.pdf
- Data publikacji:
- 2004
- Wydawca:
- Polskie Towarzystwo Biochemiczne
- Tematy:
-
AMP-deaminase
smooth muscle - Opis:
- 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.
- Źródło:
-
Acta Biochimica Polonica; 2004, 51, 1; 213-218
0001-527X - Pojawia się w:
- Acta Biochimica Polonica
- Dostawca treści:
- Biblioteka Nauki
Artykuł