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Biomedical subjects

M A Khaled

Publications and source records attributed to M A Khaled.

At least 37 records · Page 2Linked to original sources
PubMed1994

Changes in body composition of malnourished children after dietary supplementation as measured by bioelectrical impedance.

Body composition was measured with bioelectrical impedance in 35 malnourished children aged 24-59 mo to investigate the effect of a 3-wk feeding supplementation. Twenty children received a high-protein diet with 15% of total energy as protein, whereas 15 children received an isoenergetic standard-protein diet with 7.5% of energy as protein. Bioelectrical impedance analysis and anthropometry were done before and after 21 d of dietary supplementation. The children fed the high-protein diet gained significantly more body weight than those receiving the standard-protein diet (1.33 +/- 0.54 vs 0.88 +/- 0.47 kg, P < 0.02). The total body water and fat-free mass determined by bioelectrical impedance analysis showed that the group fed the high-protein diet increased significantly more (0.92 vs 0.58 kg) than those on the standard-protein diet (P < 0.02). Results of this study suggest that feeding a high-protein diet accelerates catch-up growth and restores the reference body composition in children recovering from malnutrition.

Body Composition↗
PubMed1993

Changes in body composition, diet, and strength of bodybuilders during the 12 weeks prior to competition.

The purpose of this study was to monitor body composition, diet, and strength in male bodybuilders (No. 6) during the 12 weeks prior to competition. Data were collected every third week and analyzed with repeated measures ANOVA (p < 0.05). Significant decreases (p < 0.01) were found in body mass (-7.3 kg) and hydrostatically determined percent fat (-5.0%), while fat-free mass showed little change. All 7 skinfold sites were reduced significantly (p < 0.01) across the 12 weeks. Ultrasound scan revealed a significant decrease in skin thickness at the biceps (p < 0.01), but no change in biceps thickness. Circumferences decreased significantly at all sites (p < 0.05) except the chest. The greatest decreases were at the waist (-6.9 cm) and hips (-4.3 cm). Maximal isometric dead-lift force decreased significantly (p < 0.05) across time (-129 N). In comparison to off-season, both higher resistance and aerobic training volumes were found during pre-competition. Nutritional analyses showed significant reductions (p < 0.05) in total kilocalories, protein, fat, and cholesterol intakes. Vitamin and mineral intakes exceeded the RDAs. The data indicate the pre-competition practices were effective in reducing subcutaneous fat stores while maintaining muscle. Finally, the onset of the pre-competition phase resulted in strength loss.

Adult↗
PubMed1992

Estimation of computerized tomography derived abdominal fat distribution.

Measurements of intra-abdominal fat (IAF) may be important since it is associated with numerous metabolic disorders. The relationship between computerized tomography (CT) measured fat distribution and densitometry measures was investigated in a sample of 61 male Caucasian subjects, aged 18 to 30 years with varying adiposity. Regression models were developed for estimating CT-derived fat of 40 men to estimate IAF. Two equations were developed to estimate IAF. The first used only anthropometric measures. Waist circumference and log chest ratio entered the equation and accounted for 67% of the variance. The second model included densitometry-measured percentage fat with the centred product of waist and hip circumferences, accounting for 73% of the variance. Regression equations were also developed to estimate subcutaneous fat area so that the ratio of IAF to subcutaneous fat might be estimated. Although subcutaneous fat could be estimated, the ratio between IAF and subcutaneous fat could not be estimated accurately. A validation of all regression equations developed for male subjects who also completed using a separate validation sample (n = 21). Only the studies with sample characteristics similar to those found in the validation sample validated satisfactorily. Results indicate that anthropometric and densitometry measures cannot be used to estimate CT-derived abdominal fat with precision, however they may be of value in health risk screening of individuals with high levels of IAF. Proper selection procedures with regard to age, adiposity, and morbidity must be used.

Adipose Tissue↗
PubMed1987

Determination of total body water by deuterium NMR.

A new deuterium nuclear magnetic resonance (2H NMR) method is described for determining total body water in humans. The method has been validated against a standard infrared absorption (IR) procedure using a tracer dose of deuterium oxide (2H2O) of approximately 10 g for each human subject. The precision and accuracy for the methods have been compared and found to be very similar. The advantages of the 2H NMR method over other presently available techniques that are based on 2H2O dilution are as follows: it is fast, accurate, needs only a small dose of 2H2O, can be done using any body fluid, and, most importantly, does not require any sample preparation.

Adult↗
PubMed1985

Association of folate molecules as determined by proton NMR: implications on enzyme binding.

The self-association in aqueous solution of folic acid (FA), 7,8-dihydrofolic acid (DHFA) and 5,6,7,8-tetrahydrofolic acid (THFA) has been studied by the use of proton magnetic resonance (1H NMR) spectroscopy. At concentrations below 10 mM, all three folates exist in (monomer)2 in equilibrium dimer equilibria with association constants (Ka) equal to 400, 66 and 14 M-1 for FA, DHFA and THFA respectively. These values decreased markedly to 157, 18 and 3 M-1, for FA, DHFA and THFA respectively, in the presence of 0.8 M KCl. The high extent of dimerization of FA is believed to impede the interaction with the active site of dihydrofolate reductase (DHFR) rendering it a poor substrate. In contrast, the DHFA with a much lower Ka is a better substrate. Conditions that lower the Ka of both FA and DHFA, (i.e., 0.8M KCl) turn them into better substrates. Based on the findings of the present study, it is also predicted that dihydro MTX may be a better inhibitor of DHFR than MTX.

Chemical Phenomena↗
PubMed1984

The case for the anticode.

The present paper will focus on the developments in our lab related to the origin of the code since the Israel meeting (1,2). Principally these items are: (a) a new set of correlations (3) which include ranked hydrophobicities of amino acids and dinucleotides; (b) binding constants (4) of Phe for the four mononucleotides; and (c) binding constants (5) of Phe, Leu, Ile, Val, and Gly for polyadenylic acid (poly A). The data continue to support a model for the origin of the code based on relationships between amino acids and their anticodons.

Amino Acids↗
PubMed1984

Binding constants of phenylalanine for the four mononucleotides.

Earlier work has shown that several properties of amino acids correlate directly with properties of their anticodonic nucleotides. Furthermore, in precipitation studies with thermal proteinoids and homopolyribonucleotides, an anticodonic preference was displayed between Lys-rich, Pro-rich and Gly-rich thermal proteinoids and their anticodonic polyribonucleotides. However, Phe-rich thermal proteinoid displayed a preference for its codonic nucleotide, poly U. This inconsistency seemed to be explained by a folding in of the hydrophobic residues of Phe causing the proteinoid to appear more hydrophilic. The present work used nuclear magnetic resonance techniques to resolve a limited question: To which of the four nucleotides does Phe bind most strongly? The results show quite clearly that Phe binds most strongly to its anticodonic nucleotide, AMP.

Adenosine Monophosphate↗
PubMed1983

Complexes of polyadenylic acid and the methyl esters of amino acids.

This report includes studies of the binding of the methyl esters of a series of amino acids to polyadenylic acid. The principal data were obtained using proton NMR; however, some additional data were obtained through the study of insoluble complexes and through ultraviolet spectroscopy. The binding constants are in the order Phe greater than Ile greater than or equal to Leu greater than Val greater than Gly, and show a direct correlation with the hydrophobicities of the amino acids. In most cases they are essentially double the binding constants found by Reuben and Polk (1980) for monomeric AMP. All of these amino acids, except Gly, have A as the middle letter of their anticodons, and Phe is the only one with XAA as its only anticodon. It has the anticodon richest in A and has the highest binding constant for A. These results, coupled with other data, continue to support a model of the origin of the code which is based on weak, but selective affinities between amino acids and their anticodons.

Amino Acids↗
PubMed1982

Solution and ion-complexed conformations of beauvericin determined by proton magnetic resonance spectroscopy.

The conformational properties of the cyclohexadepsipeptide antibiotic Beauvericin have been investigated by 1H-NMR spectroscopy in polar (C2H3O2H) and non-polar (CCl4, C62H6, C2HCl3) solvents and in two solvent mixtures; one a mixture of a polar and non-polar solvent (C2H3O2H/CCl4) and the other an aromatic solvent in a non-polar environment (C62H6/CCl4). The ion-complexation properties of Beauvericin with alkali metal halides (Li+, Na+, K+, Cs+) have also been studied. It is demonstrated that changes in chemical shifts of Beauvericin with concentration, with polarity of solvent or with added alkali metal ion reflect changes not only in the solvent properties but also changes in backbone conformation and changes due to ion-complexation, where appropriate, and therefore cannot be used, by themselves, to determine the conformation of the molecule, its self-aggregation properties, or the stoichiometry of the metal ion-complex. The backbone conformations of Beauvericin in different environments are determined by methods that are independent of chemical shift analysis; i.e., by measurements of 5J(HH) magnitudes observed between the alpha-CH protons of the L-phenylalanine and D-hydroxyisovaleric acid (DHyIv) residues and by nuclear Overhauser effect measurements observed between alpha-CH(HyIv) and (N)-CH3(Phe) proton signals. In the knowledge of these results the chemical shifts of Beauvericin in different environments can then be rationalised. It is found that the conformation of Beauvericin in a polar solvent is different from that found in a non-polar solvent and from that found for the in the ion-complexed form is similar to that found in non-polar solvents. By taking into account the conformational properties of the L-phenylalanine and DHyIv side-chains, it is possible to assign unambiguously the magnetically non-equivalent beta-CH2(Phe) and gamma Me(HyIv) proton signals and so elucidate the complete conformational behaviour of the uncomplexed forms of Beauvericin in a polar and a non-polar environment, and of the ion-complexed form of Beauvericin in a polar solvent.

Anti-Bacterial Agents↗
PubMed1981

Conformation characterization of cyclopentapeptide, L.Val-L.Pro-Gly-L.Val-Gly: a repeating analogue of elastin.

The cyclopentapeptide, L.Val1-L.Pro2-Gly3-L.Val4-Gly5, was synthesized and its conformational characterization was carried out using n.m.r. and theoretical energy calculations. The n.m.r. studies indicated the existence of a cis Val1-Pro2 peptide bond in water and a very strong intramolecular H-bond between the val1 NH and Gly3 C=O groups. This H-bond forms a beta-turn (type II) placing Val4 and Gly5 residues within the turn. Two minimum energy conformations were derived, one of which agrees very well with the solution conformation.

Amino Acid Sequence↗
PubMed1980

15N-NMR of repeat peptides of tropoelastin. The tetrapeptide.

The 15N-NMR data obtained in chloroform and methanol are reported for Boc-L-Val1-L-Pro2-Gly3-Gly4-OMe, a repeat tetrapeptide sequence of tropoelastin. Deuterium substitution for labile peptide protons was carried out to delineate solvent-exposed and solvent-shielded peptide nitrogens. Solvent perturbation of the peptide nitrogen resonances together with the hydrogen-deuterium substitution reaffirms the previously derived conformation of the molecule in chloroform which contains a beta-turn (type II) and a 14-membered hydrogen bond to form a cross-beta structure.

Chloroform↗
PubMed1980

Rate theory calculation of gramicidin single-channel currents using NMR-derived rate constants.

By means of 23Na NMR, two ion binding sites were observed in phospholipid-packaged gramicidin channels and the four associated rate constants were approximated. Limits also were placed on a fifth rate constant for an intrachannel ion translocation. By using Eyring rate theory to introduce voltage dependence, these rate constants were used in steady-state-current equations for calculation of gramicidin single-channel currents for two- and three-site models. Calculated single-channel currents are compared with previously published experimental single-channel currents obtained by electrical measurements on Na+ transport across gramicidin-doped planar lipid bilayers. The calculated results for the two- and three-site models compare favorably with the experimental results. Accordingly, it is demonstrated that NMR-derived rate constants can be coupled with Eyring rate theory to calculate currents through a transmembrane channel and to do so within levels of variation that compare with the differences obtained on planar lipid bilayers formed with different lipids.

Binding Sites↗
PubMed1979

Nuclear magnetic resonance studies on a cyclic dodecapeptide analogue of a repeat hexapeptide of tropoelastin: evaluation of secondary structure.

The cyclododecapeptide, (Ala1-Pro2-Gly3-Val4-Gly5-Val6)2, was synthesized and its secondary structure was evaluated from extensive studies in dimethyl sulphoxide, trifluoroethanol and water using NMR methods. A selective decoupling technique in 13C-NMR has been utilized in order to assign the C=O carbon resonances. Temperature dependence of the peptide NH protons and the solvent perturbation of the peptide NH and C=O resonances show the occurrence in all solvents of a beta-turn (a 10-membered H-bond between the Val4 NH and Ala1 C=O) and a gamma-turn, an 11-membered H-bond between the Gly3 NH and the Gly5 C=O; and a possible 14-membered H-bond between the Ala1 NH and the Val4 C=O in dimethyl sulphoxide and trifluoroethanol. These secondary structural features are compared with the linear polyhexapeptide and found the the beta-turn and the gamma-turn are the common conformational features of these peptide systems.

Amino Acid Sequence↗