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71.
72.
Effect of experimental diabetes on glycolytic intermediates and regulation of phosphofructokinase in rat lens 总被引:1,自引:0,他引:1
A M Gonzalez M Sochor P McLean 《Biochemical and biophysical research communications》1980,95(3):1173-1179
The pattern of glycolytic intermediates in the lens of alloxan-diabetic rats was indicative of regulation at phosphofructokinase. The changes in metabolites influencing phosphofructokinase activity in the diabetic, relative to the normal, rat lens were: glucose 6-phosphate, 182%; fructose 6-phosphate, 107%; fructose diphosphate, 57%. There was also a marked decrease in phosphoenolpyruvate, pyruvate, lactate and ATP but no significant change in other triose phosphates or cyclic AMP. The resuts are considered in relation to the early changes in [Ca2+] known to occur in lens in diabetes and to the coordinating effect of fructose diphosphate on flux through the glycolytic route. 相似文献
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E S Kang R E Gates T M Chiang A H Kang 《Biochemical and biophysical research communications》1979,86(3):769-778
Intact adipocytes exhibit ectoprotein kinase activity as reflected by their ability to catalyze the transfer of the terminal phosphate of (γ-32P) ATP to histone added to a cell suspension. This activity is substrate, time and cell number dependent. Lineweaver-Burk plots gave Km and Vmax values for ATP of 5 × 10?5 M and 7.14 pmoles/min/1.5 × 105 cells. Cyclic AMP but not cyclic GMP in μM concentrations stimulates ectoprotein kinase activity. The controlled tryptic digestion of intact cells results in reduction of ectoprotein kinase activity. This activity is not due to leakage of intracellular protein kinases during the preparative procedure nor to penetration of histone into the cells. Additional phosphoproteins not accessible to endogenous protein kinase activity are also localized on the external surface of the intact fat cell. 相似文献
75.
D J Takemoto S A Kaplan M M Appleman 《Biochemical and biophysical research communications》1979,90(2):491-497
The cyclic adenosine 3′,5′-monophosphate (cyclic AMP) phosphodiesterase from human leukemic lymphocytes differes from the normal cell enzyme in having a much higher activity and a loss of inhibition by cyclic guanosine 3′,5′-monophosphate (cyclic GMP). In an effort to determine the mechanism of these alterations, we have studied this enzyme in a model system, lectin-stimulated normal human lymphocytes. Following stimulation of cells with concanavalin A (con A) the enzyme activity gradually becomes altered, until it fully resembles the phosphodiesterase found in leukemic lymphocytes. The changes in the enzyme parallel cell proliferation as measured by increases in thymidine incorporation into DNA. The addition of a guanylate cyclase inhibitor preparation from the bitter melon prevents both the changes in the phosphodiesterase and the thymidine incorporation into DNA. This blockage can be partially reversed by addition of 8-bromo cyclic guanosine 3′,5′-monophosphate (8-bromo cyclic GMP) to the con A-stimulated normal lymphocytes. These results indicate a possible role of cyclic GMP in a growth related alteration of cyclic AMP phosphodiesterase. 相似文献
76.
S Nagao Y Suzuki Y Watanabe Y Nozawa 《Biochemical and biophysical research communications》1979,90(1):261-268
A Ca2+-binding protein (TCBP), which was isolated from , enhanced about 20-fold particulate-bound guanylate cyclase activity in cells in the presence of a low concentration of Ca2+, while the adenylate cyclase activity was not increased. The enhancement was eliminated by ethylene glycol-bis (β-aminoethyl ether)-N,N′-tetraacetic acid. The enzyme activity was not stimulated by rabbit skeletal muscle troponin-C, the Ca2+-binding component of troponin, or other some proteins. In the presence of TCBP, stimulating effect of calcium ion on the enzyme activity was observed within the range of pCa 6.0 to 4.6, and was immediate and reversible. 相似文献
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79.
Effect of sodium butyrate on mammalian cells in culture: A review 总被引:10,自引:0,他引:10
Kedar N. Prasad Pramod K. Sinha 《In vitro cellular & developmental biology. Plant》1976,12(2):125-132
Summary Sodium butyrate produces reversible changes in morphology, growth rate, and enzyme activities of several mammalian cell types
in culture. Some of these changes are similar to those produced by agents which increase the intracellular level of adenosine
3′,5′-cyclic monophosphate (cAMP) or by analogs of cAMP. Sodium butyrate increases the intracellular level of cAMP by about
two fold in neuroblastoma cells; therefore, some of the effects of sodium butyrate on these cells may in part be mediated
by cAMP. Sodium butyrate appears to have properties of a good chemotherapeutic agent for neuroblastoma tumors because the
treatment of neuroblastoma cells in culture causes cell death and “differentiation”; however, it is either innocuous or produces
reversible morphological and biochemical alterations in other cell types. 相似文献
80.