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Regulation of fructose-2,6-bisphosphate content in mantle tissue of the sea mussel Mytilus galloprovincialis

I. Purification and properties of 6-phosphofructo-2-kinase

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Abstract

6-phosphofructo-2-kinase (PFK-2) from the mantle of the sea mussel Mytilus galloprovincialis Lmk, collected from the Ría de Arosa (NW Spain) in 1990, was purified 550-fold by extraction and sequential affinity chromatography on Affi-gel Blue and ATP-agarose columns. The enzyme was a dimer with a native molecular weight of 100 kilodaltons (KDa) and a subunit M r of 53 KDa. PFK-2 activity is dependent on the presence of Pi. At physiological Pi concentrations, the enzyme exhibits hyperbolic kinetics with both ATP and Fru-6-P, with K m values of 0.62 and 0.37 m M respectively. In vivo, PFK-2 activity is limited by the concentration of Fru-6-P which is low in comparison with the K m for this substrate. Citrate and PEP inhibited PFK-2 activity.

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Communicated by O. Kinne, Oldendorf/Luhe

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Vazquez-Illanes, M.D., Barcia, R., Ibarguren, I. et al. Regulation of fructose-2,6-bisphosphate content in mantle tissue of the sea mussel Mytilus galloprovincialis . Mar. Biol. 112, 277–281 (1992). https://doi.org/10.1007/BF00702472

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