IgG binding and expression of its receptor in rat intestine during postnatal development.

The binding of 125I labelled IgG to the microvillus membranes (MVM) has been studied during postnatal development of rat intestine. The levels of mRNA encoding IgG receptor were also analyzed by liquid hybridization under these conditions. The IgG binding to MVM reached maximum levels by day 12 and showed a gradual decline upon weaning. The FcRn mRNA was markedly low in adult rats and was maximum during second week of postnatal development. Administration of cortisone or thyroxine to suckling rats, induced precocious decline of both IgG binding and the receptor expression. However, insulin administration did not affect the receptor expression. Scatchard analysis of IgG binding to MVM in cortisone injected pups revealed that the observed inhibition in IgG binding was a consequence of a decrease, both in the affinity constant (-Ka) as well as in the number of receptor sites (n) while thyroxine administration caused a reduction in the number of receptor sites from 2.29 in control to 1.14 nmoles/mg protein in thyroxine injected pups. These observations indicate that expression of IgG receptor during postnatal development is a hormone regulated process.

Effect of sodium on Saccharomyces cerevisiae invertase activity.

Effect of Na+ ions on yeast invertase activity has been studied as a function of pH. At acidic pH, Na+ (5-100 mM) had no effect but invertase activity was inhibited (38-44%) by Na+ ions (100 mM) with an increase in pH (6.8 and 8.0). Kinetic analysis revealed that invertase inhibition by Na+ ions was non-competitive and reversible in nature. Value of K(m) remained unaltered (33.3 mM) in presence of Na+ (20-100 mM) while Vmax decreased by 21-44% under these conditions. Value of Ki was of the order of 85 mM. Mechanism of observed inhibition of invertase activity as a consequence of Na+ ions interactions at the active site of the enzyme has been described.

Harmaline interactions with yeast invertase.

The effect of harmaline, a plant alkaloid has been studied on yeast invertase activity in the absence and presence of 50mM Na+ as a function of pH. Harmaline (1-3 mM) inhibited the invertase activity at pH 5.2, 6.8 and 8 both in the absence (44-92%) and (22-85%) of Na+ ions. Kinetic analysis revealed that harmaline is a non-competitive inhibitor of invertase, at pH 5.2 and 6.8 but at pH 8, it produced a mixed type of inhibition, Km increased by 450% and 175% and Vmax decreased by 82% and 63% in the absence and presence of 50mM Na ions respectively. The observed inhibition of invertase by harmaline was reversible in nature. These findings suggest that the presence of Na+ site is not a prerequisite for the inhibition of enzyme by harmaline.