1 research outputs found
Effect of diet of Varying Protein concentrations on the Activity of Erythrocyte Membrane Ca2+Mg2+ ATPase in Dogs
Alterations in protein diet have been reported to result in alterations
in calcium homeostasis in the body. Ca2+Mg2+ATPase is an ubiquitous
enzyme important in calcium homeostasis in the body. The effect of
varying protein diet on the activities of Ca2+ pump across cell
membranes is however yet to be fully elucidated. In this study, the
activity of erythrocyte membrane calcium pump in response to varying
protein concentration in diet was therefore studied in the dog. The
study was carried out in 24 dogs, randomly divided into 4 groups. The
groups were fed with diets containing 30%, 26%, 16% and 0% proteins
(high, medium, low and zero) for six weeks respectively. Blood samples
were collected from each animal to determine packed cell volumes,
hematocrit, blood urea, electrolyte studies and erythrocyte ghost
membrane studies. The effects of Ca2+ and ATP on the activity of
Ca2+Mg2+ ATPase were determined in the isolated ghost membrane. The
result of the study shows that there was a protein diet dependent
increase in the activity of Ca2+Mg2+ ATPase in the presence and absence
of ATP in all the groups with the highest activity recorded in the high
protein diet group and the lowest activity observed in the zero protein
group. There was also a protein diet dependent increase in the protein
concentration of the membranes in all groups observed with the highest
protein concentration recorded in the high protein diet group and the
lowest activity observed in the zero protein group.. There was a
significant decrease in K+ concentration (P<0.05) and a significant
increase in urea concentration of animals fed with high protein diet
(P<0.05). There was also a significant increase (P<0.05) in HCO3-
concentration in the animals fed with medium protein diet and no
significant difference in the PCV and heamatocrit values in all groups.
This study has shown that high protein diets increase the activity of
the Ca2+Mg2+ ATPase in the presence and absence of ATP