Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. L-asparaginase from M. phlei was purified about 170-fold with an 11% yield. The purification procedure consisted of: fractionation with ammonium sulphate; adsorption of contaminating proteins on calcium phosphate gel; chromatography on Sephadex G-150 and DEAE-cellulose. The specific activity of the final preparation was 32.6 i.u./mg protein. 2. Molecular weight of the enzyme as determined by Sephadex G-100 filtration amounted to 126 000. Optimum pH was 8.8-9.2. The enzyme did not hydrolyse L-glutamine over the pH range 4-9, and was inhibited by D-asparagine. The apparent Michaelis constant for L-asparagine was 0.7 mM; energy of activation, 9800 cal/mole. 3. On polyacrylamide-gel electrophoresis the final preparation revealed two protein bands, one of which was coincident with the enzyme activity.
Acta Biochim Pol 1976
PMID:Purification and properties of L-asparaginase from Mycobacterium phlei. 0 91

General first-order rate constants for autoxidation of sulfadiazine, sulfamerazine, sulfadimidine, sulfaperine and sulfamethoxydiazine in the air oxygen atmosphere, in solutions of pH 4-7, at 403, 411 and 418 K were determined from the absorbance measurements in 0-1 mole/dm3 HCl at 243 or 333 nm, using the so-called "subtraction technique". The thermodynamic parameters of this reaction were determined (deltaHa, deltaH not equal to, deltaS not equal to, deltaG not equal to and logA). The effect of the substituents in positions 4, 5 and 6 of the pyrimidine ring on the rate of autoxidation was interpreted in terms of the Hammett equation.
Pol J Pharmacol Pharm
PMID:Kinetics and mechanism of degradation of some 2-sulfanilamidopyrimidine derivatives. Part III. The use of Hammett equation for kinetic investigation of 2-sulfanilamidopyrimidine derivatives autoxidation. 2 Jun 12

1. The K+ transport in erythrocytes induced by gramicidin A or valinomycin is a first-order reaction. The activation energy of the induced transport is low and amounts to 6 and 10 kcal/mole, respectively. The indirect method for calculation of the driving force of diffusion, c, is given; in pig erythrocytes the c value for gramicidin A is 21.7, and for valinomycin 35.4 mM-KCl. 2. The valinomycin-induced transport was found to be the same in erythrocytes and biomolecular lipid membranes. The gramicidin A-induced transport corresponds to that of a single gramicidin channel, and not to the multichannel transport observed in the model systems. 3. Erythrocytes of various mammals show large differences in sensitivity to the ionophores. No correlation could be found between membrane lipids and the induced permeability. The role of membrane proteins in ionophore-induced permeability is discussed.
Acta Biochim Pol 1975
PMID:The influence of gramicidin A and valinomycin of the permeability of mammalian erythrocytes. 5 13

Phytase was purified from Aspergillus niger culture fluid by molecular sieve filtration on Sephadex G-200, followed by thermal inactivation of acid phosphatase and CM-cellulose chromatography. The 12-fold purified enzyme had two pH optima at 2.7 and 5.5 and was characterized by high thermal stability in alkaline environment and broad substrate specificity. The Michaelis constant of phytase relative to myo-inositol hexaphosphate sodium salt is 4.8 X 10(-4) M and activation energy 9,217 cal/mole. The molecular weight of the enzyme is estimated at 200,000.
Acta Microbiol Pol 1978
PMID:Some properties of partially purified phytase from Aspergillus niger. 7 23

General, k, and specific, k1 and k2, first-order rate constants for the parallel reaction of hydrolysis catalized by H+ ions were estimated for sulfadiazine (I), sulfamerazine (II), sulfadimidine (III), sulfaperine (IV) and sulfamethoxydiazine (V), hydrolyzed in 1 mole/dm3 HCl at 333, 343, 355 and 363 K. General first-order rate constants for the spontaneous hydrolysis of I--V in borate buffer pH 9.20 at 403, 411 and 418 K were also determined. Thermodynamic parameters of the reaction (delta Ha, deltaH not equal to, deltaS not equal to, deltaG not equal to and log A) were calculated. The effect of substituents in positions 4, 5 and 6 of the pyrimidine ring on the rate of hydrolysis was interpreted in terms of Hammett equation.
Pol J Pharmacol Pharm
PMID:Kinetics and mechanism of degradation of some 2-sulfanilamidopyrimidine derivatives. Part VI. The use of Hammett equation for kinetic investigation of 2-sulfanilamidopyrimidine derivatives hydrolysis. 60 Aug 68

Bovine serum albumin has two different binding sites for sulfonylurea. The sites at high affinity can bind up to 2 moles of a new hypoglycemic sulfonylurea SPC-703 (k1=6.8.10(3) M(-1)) or tolbutamide K1=19.3.10(3) M(-1)). The sites of lower affinity can bind 4 mole of SPC-703 (K2=1.6.10(3) M(-1)) or 8 moles of tolbutamide (k2=1.3.10(3) M(-1)). Binding of SPC-703 and tolbutamide was decreased mostly in the presence of sulfadimetoxine, but this sulfonamide increased the concentration of free tolbutamide more than that of SPC-703.
Pol J Pharmacol Pharm 1976
PMID:Influence of some salicylates and sulfonamides on binding by albumin of SPC-703 and tolbutamide. 94 61

Phosphorylation of yeast ribosomal proteins has been demonstrated in vivo and in vitro. 32-P-labelled product represents an ester-linked class of phosphoprotein. Acrylamide-gel electrophoresis has shown that in both types of experiments radioactive proteins migrate similarly; this might indicate that closely related groups of proteins become phosphorylated in vivo and in vitro. In the presence of [32-P] ATP the amount of covalently bound phosphate was 1.0 - 1.2 moles/mole of ribosome. The phosphorylation of ribosomal proteins did not appreciably affect the activity of ribosomes in a cell-free protein-synthesizing system containing poly(U) and elongation factors.
Acta Biochim Pol 1975
PMID:An in vivo and in vitro phosphorylation of yeast ribosomal proteins. 109 43

The average values of Vm and Michelis constant Km were determined for enzyme isolated from liver (12.23 mumole/min and 3.2 x 10(-6) mole/dm3. respectively). The enzyme was stable over four months at -20 degrees C. Dissociation constant enzyme-inhibitor (methotrexate) complex Ki is 3.7 x 10(-8) mole/dm3. The reaction rate was sensitive to temperature (5 degrees C increase doubled maximum reaction rate).
Acta Pol Pharm 1991
PMID:[Examining the activity of dihydrofolate reduction obtained from beef liver]. 166 36

A 22-year old patient with Jadassohn's naevus phacomatosis affecting the right side of the head, face and brain is reported. Besides naevus linearis on the forehead, lipomata of the right palpebra, skin and palate, 2 odontomata, hypodermal and submucosal hyperplasia of the right half of the oral cavity, a small aneurysm of the internal carotid artery in the cavernous sinus and linear calcification in the cortex of the medial surface of the occipital lobe like those in Sturge-Weber disease were found. Clinically, she was found to be mentally retarded (moderately) and having epilepsy. Epileptic attacks occurred up to the age of 13 years, while changes in EEG are still present.
Neurol Neurochir Pol
PMID:[A case of epidermal nevus (Jadassohn's phacomatosis) with changes in the nervous system]. 180 60

Dextromoramide and pethidine were separated and identified by thin-layer chromatography on silica gel, using ammonia and methanol (1.5:100) as the mobile phase, after previous extraction with dicthyl ether or with a mixture of n-hexane and isoamyl alcohol (98.5:1.5) from blood alkalized to pH 10.3 Dextromoramide can be revealed on the chromatograms in the amount of 0.5 micrograms and pethidine in the amount of 1 micrograms using the Dragendorff reagent. Reversed-phase TLC proved less sensitive. High-performance liquid chromatography on the column of LiChrosorb RP-18 was applied to the determination of dextromoramide in blood after extraction with diethyl ether, using methanol--phosphate buffer pH 4.5 (95:5) as the mobile phase. The determination range was of 0.5-5.0 micrograms per 2 cm3 of blood plasma (1.26.10(-8)-1.26.10(-7) mole/dm3).
Acta Pol Pharm 1989
PMID:[Chromatographic identification and analysis of dextromoramide in the plasma by the method of high performance liquid chromatography]. 263 68


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