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81.
M Alam M Ahmad A Rasheed M Saleem M K Javaid S Ikram 《Indian journal of experimental biology》1990,28(10):940-942
The metabolic fate of isatin hydrazone (Ia), isatin-3-thiosemicarbazone (Ib), isatin-3-semicarbazone (Ic), isatin-3-phenylhydrazone (Id), isatin oxime (Ie) and 3-hydroxy-3-acetonyl oxindole (II) was studied in rabbits. The compounds were administered orally in the dose of 300 mg/kg body wt. Isatin anthranilic acid, tryptophan and nicotinic acid were identified as the major metabolites excreted in urine. The 3-hydroxy-3-acetonyl oxindole (II) gave on additional metabolite, oxindole. The major metabolites were separated and identified unambiguously on thin layer silica gel plate. Metabolic pathways have been proposed to explain the biotransformation of the compounds investigated. 相似文献
82.
Three enzymes involved in the conversion of 3T3-L2 fibroblasts into fat cells, acetyl CoA carboxylase (ACC), fatty acid synthetase (FAS) and pyruvate carboxylase (PC) have been localized by immunofluorescence techniques. The method enables the identification of cells undergoing the conversion while they are still fibroblastic in appearance, often before the obvious appearance of fat droplets. Specific fluorescence for each enzyme can be seen in "clones" of cells derived from single cells, which may undergo an event during logarithmic growth, which programs the cells to differentiate subsequent to confluence of and addition of induction medium. 相似文献
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An acyl coenzyme A (CoA) carboxylase, which catalyzes the adenosine triphosphate-dependent fixation of CO2 into acetyl-, propionyl-, and butyryl-CoA, was detected in fractionated cell extracts of Propionibacterium shermanii. Catalytic activity was inhibited by avidin but was unaffected by avidin pretreated with excess biotin. The carboxylase levels detected were relatively small and were related to cellular growth. Maximal carboxylase activity was detected in cells grown for about 96 h. Thereafter, the activity declined rapidly. Optimal CO2 fixation occurred at pH 7.5. Other parameters of the assay system were optimized, and the apparent Km values for substrates were determined. The end product of the reaction (with acetyl-CoA as the substrate) was identified as malonyl-CoA. The stoichiometry of the reaction was such that, for every mole of acetyl-CoA and adenosine triphosphate consumed, 1 mol each of malonyl-CoA, adenosine diphosphate, and orthophosphate was formed. These data provide the first evidence for the presence of another biotin-containing enzyme, an acyl-CoA carboxylase, in these bacteria in addition to the well-characterized methylmalonyl-CoA carboxyltransferase. 相似文献
86.
The irreversible unfolding of covalently inhibited swine pepsin by urea was studied by spectrophotometric and viscosity measurements. At pH 4.5 and 25 degrees C in 8 M urea, a stable intermediate form of the protein was detected. It differed from the native protein by a slight loss of secondary structure and an increased intrinsic viscosity ([pi] = 7.5 mL g-1), indicating the intermediate to have an increased molecular volume or to be more asymmetric in shape. The protein was transformed into a random coil form by increases of temperature and pH. Comparison with other results suggested that at pH 6 pepsin is less stable than its inactive precursor, pepsinogen, by about 3 Kcal mol-1 (1 cal = 4.187 J). 相似文献
87.
This investigation reports observations on the growth of Rana cyanophlyctis tadpoles following a whole body gamma-ray exposure. The effect on the body and hind limb size is perhaps the most significant of the period of latency. A dose of 2,000 R serves as a stressor and activates ACTH secretion in the tadpoles. The resultant somatotrophic hormone (STH) inhibition and subsequent recovery during the following days seem an integral part of the radiation syndrome. 相似文献
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The denaturation of swine pepsinogen has been studied as a function of urea concentration, pH, and temperature. The unfolding of the protein by urea has been found to be fully reversible under different conditions of pH, temperature, and denaturant concentration. Kinetic experiments have shown that the transition shows two-state behavior at 25 degrees C in the pH range 6-8 covered in this study. Analysis of the equilibrium data obtained at 25 degrees C according to Tanford (Tanford, C. (1970), Adv. Protein Chem. 24, 1) and Pace (Pace, N.C. (1975), Crit. Rev. Biochem. 3, 1) leads to the conclusion that the free energy of stabilization of native pepsinogen, relative to the denatured state, under physiological conditions, is only 6-12 kcal mol-1. The temperature dependence of the equilibrium constant for the unfolding of pepsinogen by urea in the range 20-50 degrees C at pH 8.0 can be described by assigning the following values of thermodynamic parameters for the denaturation at 25 degrees C: deltaH=31.5 kcal mol-1; deltaS=105 cal deg-1 mol-1; and deltaCp=5215 cal deg-1 mol-1. 相似文献
90.
Alcohol dehydrogenase was prepared from 2-day germinating maize and 3-day germinating broad-bean seeds by ammonium sulphate fractionation of sodium phosphate extracts, chromatography onDEAE cellulose and Sephadex G-200. The activity of the broad beanADH amounted to182 800 units per mg protein, that of maizeADH 79 000 units per mg protein. Besides oxidation of a series of alcohols at pH optimum in the alkaline region and with KM equalling 10-2M, alcohol dehydrogenases isolated from both plants catalyze the reduction of acetaldehyde, n-propanal, n-butanal, isobutanal and crotonal at pH optimum in the neutral region with KM equalling 10-3M. The inhibition studies using fatty acids and chloride ions revealed that the oxidation of alcohols is inhibited competitively by both types of inhibitors, with inhibition constants of 10-2M and 10-1M, respectively. The inhibition in the presence of acetaldehyde is non-competitive since the inhibitors do not compete with acetaldehyde and do not form an enzyme-NADH-inhibitor complex, yet they obviously react with the enzyme-NAD product only, thus giving rise to an enzyme-NAD-inhibitor complex. These differences in the behaviour of inhibitors may be interpreted in the sense that the binding sites of ethanol and acetaldehyde as substrates for broad bean and maize alcohol dehydrogenases are non equivalent. The nonequivalency discussed in the text. 相似文献