Properties of renal fructose 1,6 bis-phosphatase of goat.

The renal fructose 1,6 bis-phosphatase was partially purified from goat kidney. The purified enzyme showed 10.5 as the pH optimum. The enzyme essentially required Mg2+ for its activity. Heavy metals inhibited enzyme activity. Inhibition was relieved by chelator EDTA and cysteine. These results suggest that renal fructose of goat, too, is sulfhydryl-requiring enzyme.

A note on adenosine triphosphatase activity in foetal goat liver, testis, allantoic and amniotic fluids.

The activity of the enzyme adenosine triphosphatase was measured in liver, testis and foetal fluids. The activity was maximum in the foetal liver and minimum in adult liver. On the other hand the activity in adult goat testis was higher than foetal goat testis.

A note on post partum utero vaginal prolapse in Gir cows: estimation of serum calcium, phosphorus, proteins, and cholesterol.

Reported are results obtained from determination of calcium, phosphorus, protein, and cholesterol in blood serum of 10 Gir cows with uterine prolapse. Particular reference is made to possible adverse effects of hypocalcaemia in conjunction with physiological stress resulting from pregnancy and parturition.

Sequential development of enzymes of gluconeogenesis and glucose synthesis in fetal goat liver.

The development of three key gluconeogenic enzymes, viz. phosphoenolpyruvate carboxykinase, fructose 1.6-bisphosphatase and glucose 6-phosphatase, and the gluconeogensis by liver slices were studied during development of goat fetus. The three enzymes develop in a sequential and time dependent manner, and the glucose 6-phosphatase develops last at around 100 days of gestation. Glucose synthesis by fetal liver slices was observed after 120 days of gestation. It may be concluded that the gluconeogenic sequence is operative well before birth and the goat fetus synthesizes its own glucose after 100 days of gestation.

Fructose 1:6 bisphosphatase activity in the liver and testis of rats and goats.

1. The activity of the enzyme Fructose 1:6 Bisphosphatase (FDPase) was studied in the liver and testis of adult goats and rats. No significant difference in the enzyme activity was observed between liver and testis of rats. Highly significant differences (P less than 0.01) were observed between the activity of goat liver and goat testis, goat liver and rat liver, goat testis and rat testis; the activities being higher in goat tissues. 2. Homogenization of the tissues with water, 0.05 M lactate buffer (pH 3.5), 150 mM KCl and 0.34 M sucrose yielded highest activity with water and lactate buffer followed by Sucrose and KCl. 3. 10 microM of Fe2+ and 45 microM of Zn2+ decreased the enzyme activity of rat testis by 39% and 93% respectively. 4. The rate of hydrolysis of FDP with respect to time in rat liver and testis was a first order reaction. Linear kinetics of the substrate hydrolysis was observed up to 90 min. No substrate inhibition of the enzyme activity was observed up to 50 microM of the substrate. Km of rat liver and testis FDPase were 8.3 microM and 10.5 microM respectively.

Kinetics of fructose utilization by buffalo spermatozoa.

Experiments have been conducted to estimate the fructolytic index, Fl (mg of fructose utilized by 10(9) spermatozoa in 60 minutes), Fructolytic Coefficient, Ku (Fractional decline in the spermatozoal fructolytic activity on an instantaneous basis), Maximum fructose utilization, MFU (mg of fructose utilized by 10(9) spermatozoa in one minute at zero incubation time on an instantaneous basis) and T 1/2 (Biological half life of semen) of buffalo spermatozoa. The effect of citrate and phosphate buffers on the measures of fructolysis, the Pasteur effect and the fructose utilization by the head, midpiece and tail fraction of spermatozoa have also been investigated. Fructolytic index of the buffalo spermatozoa has been compared with those of exotic bulls. Fl was highly significantly different between first, second and third hour of incubation. Significant correlations were obtained between sperm concentration and fructose utilization in all the 20 minute periods. Ku was independent of initial fructose concentration (IFC) sperm concentration and the incubation period. The Fructose utilization followed a first order reaction. The correlation coefficient between the seminal attributes and different measures of fructolysis have been presented. All the measures of fructolysis were significantly higher in citrate buffer as compared to phosphate buffer. None of the fractions of the spermatozoa showed fructolytic activity on incubation with exogeneous fructose.