Sodium- and potassium-dependent adenosine triphosphatase activity in a rat-kidney endoplasmic reticulum fraction

1963 ◽  
Vol 71 ◽  
pp. 266-276 ◽  
Author(s):  
Erwin J. Landon ◽  
John L. Norris
1966 ◽  
Vol 100 (3) ◽  
pp. 762-767 ◽  
Author(s):  
N Gruener ◽  
Y Avi-Dor

1. The adenosine-triphosphatase activity of rat-brain microsomes was measured between 0 degrees and 37 degrees . The stimulatory effect of Na(+) plus K(+) on the Mg(2+)-dependent adenosine-triphosphatase activity decreased sharply with decreasing temperature and became negligible at 0 degrees . An Arrhenius plot drawn from the experimental data showed two discontinuities: one at about 6 degrees and the other at about 20 degrees . 2. The increment in activity induced by Na(+) plus K(+) was more sensitive to oligomycin at lower than at higher temperatures, but the opposite was observed for ouabain. The action of oligomycin showed a biphasic character, since below a certain concentration it caused slight activation of Na(+)-plus-K(+)-activated adenosine triphosphatase. 3. Where oligomycin increased the activity of the enzyme, it also enhanced the accumulation of an acid-precipitable phosphorylated compound formed through the transfer of the gamma-phosphate group of [(32)P]ATP to the enzyme system. Stimulatory concentrations of oligomycin did not interfere with K(+)-mediated dephosphorylation of the intermediate, though high concentrations of oligomycin counteracted the effect of K(+). 4. The temperature profile of K(+)-stimulated microsomal phosphatase qualitatively resembled that of microsomal adenosine triphosphatase.


1965 ◽  
Vol 13 (1) ◽  
pp. 44-56 ◽  
Author(s):  
MAX WACHSTEIN ◽  
MAIRE BRADSHAW

The activities of various enzymes were studied histochemically in two species which at birth have a kidney with an active nephrogenic zone, the rat and rabbit, and one (the guinea pig) in which this organ is at this time apparently fully matured. The histochemical reactions, in general, reflect the degree of maturity found in kidneys of newborn and growing animals. Immature proximal convoluted tubules lack enzymatic activity or show only minimal amounts. As these tubules mature, the adult pattern is noted at about the 14th to 16th day after birth in rat, and after 21 to 28 days in rabbit. Within this general pattern, however, considerable variations are noted. Glucose-6-phosphatase, e.g., is less active at birth, even in mature tubules, while acid phosphatase localized in granular "lysosomal" bodies is as prominent in newborn kidney as in adult. Newborn guinea pig kidney lacks glomerular adenosine triphosphatase activity in spite of its general enzymatic maturity, while rat kidney at birth has no tubular adenosine triphosphatase activity, even in more mature proximal convolutions. Oxidative enzymes, particularly succinic dehydrogenase, and acid phosphatase are active in tubules of the inner portion of medulla in rat and rabbit at birth. This appears to be an expression of the immaturity of newborn kidney. With the progress of zonal differentiation, this enzyme activity is no longer found in the papillary portion of medulla where thin limbs of Henle's loop are now located. In rat kidney, best seen in cryostat sections briefly postfixed in very cold neutral formalin, single cells are found in the collecting ducts with striking 5-nucleotidase activity. The number of these cells is greater in neonatal kidney than in adult kidney. The physiological significance of many of the findings described in this report has still to be clarified.


Sign in / Sign up

Export Citation Format

Share Document