The effect of different levels of bengal gram protein containing normal and subnormal amounts of calcium on protein biosynthesis in vitro in rat intestinal mucosa calcium atpase activity and on serum calcium


Khan, A.; Chakrabarti, C.H.

Indian Journal of Nutrition and Dietetics 23(9): 262-268

1986


The effect of different levels of bengal gram protein containing normal and subnormal amounts of calcium has been investigated on incorporation of 14C-leucine into proteins of crude microsomal fractions of the rat intestinal mucosa in vitro and on serum calcium and calcium dependent ATP-ase activity for 3 weeks and 8 weeks. The reduced incorporation of 14C-leucine into proteins of crude microsomal fractions of intestinal mucosa of protein malnourished rats indirectly indicate the reduced activity of calcium bound protein which is intimately associated with the calcium absorption in rats. The administration of oral dose of calcium chloride solution two hours before killing the animals fed 18 percent pulse protein with low amount of calcium resulted in the significant increase in the serum calcium. This has been attributed to the fact that in these animals there is already normal synthesis of protein because of availability of appropriate amino acids and extra administration of calcium presumably resulted in the increased absorption of calcium associated with the increased levels of serum calcium within the normal physiological range. The activity of Ca2+-ATP-ase has lowered significantly in the animals fed 6 percent and 12 percent pulse protein containing normal and subnormal amounts of calcium for three and eight weeks, when compared with control animals. The reduced ATP-ase activity in these animals has been attributed to the insufficient availability of amino acids to synthesize apoprotein part of the enzyme. The lower activity of ATP-ase in the animals fed 18 percent pulse protein with low amounts of calcium has been attributed to the low amount of calcium not sufficient to stimulate the activity of calcium dependent ATP-ase.