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. Author manuscript; available in PMC: 2009 Sep 1.
Published in final edited form as: Biochim Biophys Acta. 2008 May 2;1784(9):1342–1346. doi: 10.1016/j.bbapap.2008.04.016

Fig. 4. Cooperativity of dependence of reaction velocity of rat liver GNMT on AdoMet concentrations in presence of 5-CH3-THF-pentaglutamate.

Fig. 4

Dependence of velocity on AdoMet concentrations is shown for GNMT apo-protein (closed circles, taken from Fig.1), GNMT-5-CH3-THF-Glu5 complex after incubation with 1 mM 5-CH3-THF-Glu5 followed by passage through Spin-Columns to remove excess folate, as described in the text (open circles), and in the presence of 1 µM 5-CH3-THF-Glu5 in the reaction mixture (open squares). Data fitted with the Hill equation.