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Comp Biochem Physiol B ; 82(4): 841-8, 1985.
Article in English | MEDLINE | ID: mdl-4092442

ABSTRACT

Pyruvate kinase of sea bass (Dicentrarchus labrax L.) shows positive cooperativity with respect to both substrates PEP and ADP. The temperature is a modulator of this activity, changing KS0.5 and Hill coefficient values for PEP. The enzyme shows alanine and ATP inhibition and F-1,6-P2 activation at 22 degrees C. F-1,6-P2 eliminates the effect of alanine but not that of ATP. These results could indicate a regulation of this enzyme by temperature and possess kinetic properties which are similar to that of L-type mammals.


Subject(s)
Liver/enzymology , Pyruvate Kinase/metabolism , Animals , Fishes , Kidney/enzymology , Kinetics , Muscles/enzymology , Myocardium/enzymology , Seawater , Substrate Specificity , Temperature , Tissue Distribution
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