Author(s)

Anita Williams, Ami Abbott, Jessica Chadwick, Alicia Thomas, Nathalia Cruz, Alice Deng, Leah Ordinanza, John Tat, Percy Russell

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Department of Medical Education, School of Medicine, University of California, Division of Biology, San Diego, USA.

Previous studies showed that rabbit muscle phosphofructokinase-1 (PFK-1) activity losses due to dilution, due to inhibition by ascorbate, and due to some lithium salts were prevented by rabbit muscle aldolase. Chicken PFK-1 and fish PFK-1 interacted with ascorbate and were inhibited, consistent with a previously proposed function that ascorbate facilitates glycogen in resting muscle by inhibiting glycolysis. This report shows that a plant enzyme, spinach aldolase, has the same ability to prevent rabbit muscle PFK-1 activity loses as rabbit muscle aldolase and in some instances it was a better protector from activity losses than rabbit aldolase. Spinach aldolase also protected chicken and fish PFK-1s from inhibitions by ascorbate and from activity losses due to dilution. Prevention of losses PFK-1 activities from animal species by a plant protein, spinach aldolase, suggests an evolutionary conservative relationship between PFK-1s and aldolases.

Phosphofructokinase-1; Spinach Aldolase Interactions; Carbonate Inhibitions; Rabbit Aldolase; Evolutionary Conservative Relationships; Ascorbate Inhibition

Williams, A. , Abbott, A. , Chadwick, J. , Thomas, A. , Cruz, N. , Deng, A. , Ordinanza, L. , Tat, J. and Russell, P. (2013) Spinach aldolase interactions with rabbit, chicken, and fish muscle phosphofructokinase-1. Advances in Enzyme Research, 1, 121-131. doi: 10.4236/aer.2013.14013.