Gene/Protein Disease Symptom Drug Enzyme Compound
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 53,079 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The transport of the amino acids, cystine and lysine, was studied in epithelial cell lines propagated from human kidney cortex. Cystine uptake data were reproducible in different cell lines and did not vary over several cell passages of an individual cell line. The transport of this disulfide amino acid was sodium-dependent with kinetic analysis showing one apparent Kt system of 0.09 mmol/L and Vmax of 0.054 mmol/L cell water/min. Studies of the kinetics of lysine transport, however, revealed two uptake systems with apparent high and low affinities with Kt of 0.14 mmol/L and 5 mmol/L and Vmax of 0.041 and 0.167 mmol/L cell water/min, respectively. Glutamate appeared to be the most potent inhibitor of cystine uptake by these cultured human renal cells and this interaction was competitive. Although cystine did not inhibit lysine uptake, arginine and ornithine were shown to be major inhibitors, thus providing evidence for the presence of a shared dibasic amino acid transport system.
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PMID:Cystine and lysine transport in cultured human renal epithelial cells. 310 30

Four 28-d trials were conducted using a total of 432 pigs, with average initial weight across trials ranging from 6.3 to 9.7 kg, to estimate the tryptophan (trials 1 and 2) and threonine (trials 3 and 4) requirements of pigs fed low protein, corn-sunflower meal diets. The effect of tryptophan, threonine and protein level on serum calcium, phosphorus and zinc also was studied. The diets contained either 12 or 13% protein and were calculated to be adequate in all nutrients except crude protein and the amino acid being investigated. A lysine supplemented, 18% protein, corn-sunflower meal diet was included in all trials as a positive control. In trial 1, weight gains of pigs increased linearly (P less than .005) while feed conversion improved cubically (P less than .05) as dietary tryptophan increased from .14 to .22%. Pigs fed the 18% protein diet gained faster (P less than .05) and required less feed/gain than pigs fed low protein diets. In trial 2, weight gains improved quadratically (P less than .005) and feed conversion improved linearly (P less than .05) as dietary tryptophan increased from .104 to .204%. Serum phosphorus and zinc concentrations were lower (P less than .05) in pigs fed the 18% protein diet. In both trials, serum urea N responded quadratically (P less than .05) to increasing dietary tryptophan, and was lower (P less than .05) in pigs that were fed diets supplemented with L-tryptophan than in those fed the low protein basal or 18% protein diets.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Tryptophan and threonine requirements of young pigs and their effects on serum calcium, phosphorus and zinc concentrations. 310 96

A nutritional quality index in the nature of an enzymatic protein efficiency ratio (E-PER) was computed from the amino acid data of 18 different food products by means of multiple regression equations. The regression was performed by setting amino acid values derived from enzymic hydrolysis of the food proteins as the independent variables with the rat-based PER values as the dependent variables. The multiple regression gave the following equation: E-PER = -3.02 + 0.14 (asp) + 0.15 (glu) - 0.18 (pro) + 0.14 (ala) + 0.52 (met) + 0.21 (lys) + 0.09 (arg) - 0.45 (trp). The multiple correlation coefficient for this regression was 0.942 and the coefficient of variation was 88.7%. The prediction equation was tested on amino acid-PER data of 22 different foodstuffs and it successfully predicted (+/- 0.22) the PER of 17 and an effectiveness of 77.3%.
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PMID:A rapid in vitro enzymic and chromatographic predictive model for the in vivo rat-based protein efficiency ratio of mixed food proteins. 323 Dec 63

Proteinase K, the extracellular serine endopeptidase (E.C.3.4.21.14) from the fungus Tritirachium album limber, is homologous to the bacterial subtilisin proteases. The binding geometry of the synthetic inhibitor carbobenzoxy-Ala-Phechloromethyl ketone to the active site of proteinase K was first determined from a Fourier synthesis based on synchrotron X-ray diffraction data between 1.8 A and 5.0 A resolution. The protein inhibitor complex was refined by restrained least-squares minimization with the data between 10.0 and 1.8 A. The final R factor was 19.1%, and the model contained 2,018 protein atoms, 28 inhibitor atoms, 125 water molecules, and two Ca2+ ions. The peptide portion of the inhibitor is bound to the active center of proteinase K by means of a three-stranded antiparallel pleated sheet, with the side chain of the phenylalanine located in the P1 site. Model building studies, with lysine replacing phenylalanine in the inhibitor, explain the relatively unspecific catalytic activity of the enzyme.
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PMID:X-ray and model-building studies on the specificity of the active site of proteinase K. 323 15

When combining angioplasty and local lysis with urokinase (UK) in treatment of peripheral arterial occlusions we have observed marked differences in the individual patient's response irrespective of the age of the thrombus. The extensive arteriosclerotic changes revealed by angiography in some of these patients suggest a reduced fibrinolytic potential depending on the underlying disease. In the standard in vitro test system we measured the UK-dependent thrombolysis in blood samples from 10 normal controls at UK concentrations of 150, 200, and 300 IU/ml of whole blood. In comparison we determined the whole blood thrombolysis time (WBTT) of 10 patients with AOD using UK concentrations of 150, 200, and 300 IU/ml of whole blood. The mean WBTT values for normal controls obtained at UK concentrations of 150 IU/ml, 200 IU/ml, and 300 IU/ml, respectively, amounted to 9.5, 5.5, and 3.5 minutes, respectively, while in patients mean values of 20.7, 8.1, and 5.5 minutes, respectively, were found. Studies on plasma samples had shown that the lysis time could be shortened in a dose-dependent manner by addition of lys-plasminogen (LYS-PLASMINOGEN Steam Treated) and to some extent also glu-plasminogen. Since lys-plasminogen gave clearly superior results we tried to improve the lytic potential in terms of a shortening of the WBTT by adding different doses of lys-plasminogen (0.14-0.56 CU/ml whole blood) to each patient sample. Although the individual response varied, the addition of lys-plasminogen to the patient samples resulted in a clear dose-dependent improvement of pathologically prolonged lysis times.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Reduced fibrinolytic potential in patients with arterial occlusive disease (AOD) in comparison with normal subjects. 335 Mar 95

The purpose of the present research was to establish the variability in agronomic, chemical and nutritional characteristics among 25 amaranth (A. caudatus) cultivars. A large variability was found among cultivars in all the parameters evaluated. Average seed weight was 0.75 mg, and had an average size of 1.23 x 1.14 mm. The average moisture, protein and fat content was 11.81, 12.66 and 8.44%, respectively. The average values for methionine, threonine, cystine, leucine and lysine were: 168, 276, 74, 381 and 370 mg/g N, in the same order as presented. It was possible to establish significant, positive correlations between yield-protein, methionine-cystine, methionine-lysine, and threonine-leucine, as well as significant negative correlations between protein-cystine, fat-methionine and cystine- leucine. Furthermore, it is not possible to select cultivars of higher yield on the basis of seed weight, since these two variables were negatively correlated, although not statistically significant. Among all 25 cultivars studied, some were deficient in sulfur-containing amino acids, while based on the FAO/WHO essential amino acid pattern, all of them were deficient in leucine. The average protein quality value expressed as NPR was 3.54 in thermally-processed samples, with no differences between cultivars. Nevertheless, protein digestibility values probably classified the samples in two groups with average values of 79 and 81%, respectively. The variability found can thus be used to select cultivars with higher yields and higher nutritional characteristics.
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PMID:[Genetic variability and correlation of yield, grain size, chemical composition and protein quality of 25 varieties of amaranth (Amaranthus caudatus)]. 345 13

Chymopapain A was isolated from the dried latex of papaya (Carica papaya) by ion-exchange chromatography followed by covalent chromatography by thiol-disulphide interchange. The latter procedure was used to produce fully active enzyme containing one essential thiol group per molecule of protein, to establish that the chymopapain A molecule contains, in addition, one non-essential thiol group per molecule and to recalculate the literature value of epsilon 280 for the enzyme as 36 000 M-1 X cm -1. The Michaelis parameters for the hydrolysis of L-benzoylarginine p-nitroanilide and of benzyloxy-carbonyl-lysine nitrophenyl ester at 25 degrees C, and I 0.1 at several pH values catalysed by chymopapain A, papaya proteinase omega, papain (EC 3.4.22.2) and actinidin (EC 3.4.22.14) were determined. Towards these substrates chymopapain A has kcat./km values similar to those of actinidin and of papaya proteinase omega and significantly lower than those of papain or ficin. The environment of the catalytic site of chymopapain A is markedly different from those of other cysteine proteinases studied to date, as evidenced by the pH-dependence of the second-order rate constant (k) for the reaction of the catalytic-site thiol group with 2,2'-dipyridyl disulphide. The striking bell-shaped component that is a characteristic feature of the reactions of S-/ImH+ (thiolate/imidazolium) ion-pair components of many cysteine-proteinase catalytic sites with the 2,2'-dipyridyl disulphide univalent cation is not present in the pH-k profile for the chymopapain A reaction. The result is consistent with the presence of an additional positive charge in, or near, the catalytic site that repels the cationic form of the probe reagent. Resonance Raman spectra were collected at pH values 2.5, 6.0 and 8.0 for each of the following dithioacyl derivatives of chymopapain A: N-benzoylglycine-, N-(Beta-phenylpropionl)glycine- and N-methoxycarbonylphenylalanylglycine-. The main conclusion of the spectral study is that in each case the acyl group binds as a single population known as conformer B in which the glycinic N atom is in close contact with the thiol S atom of the catalytic-site cysteine residue, as is the case also for papain and other cysteine proteinases studied. Thus the abnormal catalytic-site environment of chymopapain A detected by the reactivity-probe studies, which may have consequences for the acylation step of the catalytic act, does not perturb the conformation of the bound acyl group at the acyl-enzyme-intermediate stage of catalysis.
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PMID:Chymopapain A. Purification and investigation by covalent chromatography and characterization by two-protonic-state reactivity-probe kinetics, steady-state kinetics and resonance Raman spectroscopy of some dithioacyl derivatives. 351 53

In order to study the utilization of urea in poultry, 3 colostomized laying hybrids were orally supplied with a traditional ration supplemented with 1% 15N'-labelled urea with a 15N excess (15N') of 96.06 atom-% over a period of 6 days. After another 2 days on which the hens received the same ration with unlabelled urea, they were butchered. The atom-% 15N' of the blood on an average of the 3 hens was 0.64, of the plasma 1.40 and of the corpuscles 0.47. The TCA-soluble fraction of the blood had an average 15N' of 1.14 atom-%; the 15N amount is 9.7% of the total amount of 15N in the blood. The amount of 15N' in the urea in the blood was 6.8 atom-%. This shows that the absorbed urea is decomposed very slowly. The quota of 15N' in the basic amino acids from the total 15N' of the blood plasma is only 0.3% and that of the corpuscles 2.2%. The average 15N' of the mature follicles is 2.39 atom-% whereas the smallest and the remaining ovary contain 1.12 atom-%. The labelling level of lysine in mature egg cells was, in contrast to this, only 0.08 atom-% 15N' and in infantile follicles 0.04 atom-% 15N'. 1% of the 15N' quota is in the follicles and the remaining ovary. Of the basic amino acids, histidine is most strongly labelled. The as a whole lower incorporation of the 15N from urea into the basic amino acids shows that the nitrogen of this compound can be used for the synthesis of the essential amino acids to a low degree only.
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PMID:[Evaluation of 15N marked urea in the laying hen. 4. Incorporation of 15N in blood, its fractions and follicles in various developmental stages]. 363 34

This study was carried out on 14 asthmatic children aged 7-13 years. They all received three preparations (aminophylline by intravenous infusion, lysine theophyllinate orally in solution and slow release theophylline orally as capsules) in a single dose of 100 mg active ingredient in a crossover design. Plasma theophylline concentrations, determined by a fluorescent polarization immunoassay, were evaluated both by compartmental and non-compartmental analysis. After administration of slow release theophylline, its maximum plasma concentration and the time needed to reach this were (+/- SD) 3.19 +/- 0.63 microgram/ml and 8.71 +/- 2.30 h, respectively, compared to 4.51 +/- 0.94 microgram/ml and 1.96 +/- 0.85 h, respectively, for the oral normal release solution. Mean absolute and relative percentage bioavailabilities for slow release theophylline in asthmatic children were (+/- SD) 92.7 +/- 23.2% and 83.14 +/- 14.69%, respectively. These are similar to the values found with other slow release formulations in paediatric patients.
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PMID:Absolute and relative bioavailability of a slow release theophylline preparation in asthmatic children. 367 95

A tridecapeptide containing tritium-labelled lysine and corresponding closely to residues 98 to 110 of the alpha chain of type I collagen was synthesized by the solid-phase method. Gly-Leu-Hyp-Gly-Nle-[4,5-3H]Lys-Gly-His-Arg-Gly-Phe-Ser-Gly was used as a substrate of human protocollagen lysyl hydroxylase (peptidyllysine, 2-oxoglutarate: oxygen 5-oxidoreductase, EC 1.14.11.4) obtained from dermal fibroblasts. L-[4,5-3H]Lysine was converted to N alpha-t-butyloxycarbonyl-N epsilon-o-chlorobenzyloxycarbonyl [3H]lysine which was incorporated during stepwise synthesis of the peptide. The chemical and radiochemical purities and specific activity of the completed peptide were characterized. A non-radiolabelled analogue of the peptide inhibited the hydroxylation of [3H]lysine-containing protocollagen by human lysyl hydroxylase, indicating that the synthetic peptide interacted with the enzyme. The peptide containing [3H]lysine was a substrate for lysyl hydroxylase and permitted direct measurement of enzyme activity in relatively crude cell extracts by a tritium-release assay. Extracts of cultured fibroblasts from a patient with an autosomal recessive pattern of inheritance for Ehlers-Danlos syndrome type VI had activities for tritium release from either the radiolabelled synthetic peptide or from [3H]lysine-containing protocollagen that were only 30% of those from control cells. These data indicate that a stable, well-defined synthetic peptide containing [3H]lysine is a useful substrate for studies of genetically variant lysyl hydroxylase from cultured human cells.
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PMID:A [3H]lysine-containing synthetic peptide substrate for human protocollagen lysyl hydroxylase. 392 29


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