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202
Chapman, J. B., K. Pohlmann, G. Pohll, A. E. Hassan, P. Sanders, M. Sanchez, and S. Jaunarajs, "Remediation of the Faultless Underground Nuclear Test: Moving Forward in the Face of Model Uncertainty", Waste Management Conference, WM'02, Session 28A, paper 456, Tucson, Arizona, USA, 24-28 February, 202.
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Miller, S. A., D. D. D., and H. F. Polesky, "(1988). A simple salting out procedure for extracting DNA from human nucleated cells.research,", Nucleic acids, vol. 16, no. (3),, 1215. Abstract
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Miller, S. A., D. D. D., and H. F. Polesky, "(1988). A simple salting out procedure for extracting DNA from human nucleated cells.research,", Nucleic acids, vol. 16, no. (3),, 1215. Abstract
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1968
Popper, K., The {Logic} of {Scientific} {Discovery}, , London, Hutchinson, 1968. Abstract
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1971
Zedan, H. H., and R. Plourde, "Spores plate method" for transformation of steroids by fungal spores entrapped in Silica Gel G. ", Appl. Microbiol. (USA) , vol. 21, pp. 815-819., 1971.
1972
DILUTION, O. F. C. A. T. T. L. E. B. Y. I. S. O. T. O. P. E., A. Pfau, and M. A. I. Salem, "Max Planck Institute for Animal Breeding and Animal Nutrition, Mariensee, Federal Republic of Germany", Isotope studies on the physiology of domestic animals: proceedings of a symposium..., vol. 309: International Atomic Energy Agency, pp. 21, 1972. Abstract
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Parnas, D., "On the criteria to be used in decomposing systems into modules", Communications of the ACM, vol. 15, pp. 1053–58, 1972. Abstract
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Pfau, A., and M. A. I. Salem, "STUDIES ON BODY COMPOSITION OF CATTLE BY ISOTOPE DILUTION ANALYSIS", Proc Symp. an Iso. study on physiol. of domest. Anim. IAEA/FAO, pp. 21-34, 1972. Abstract
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Pfau, A., and M. A. I. Salem, "STUDIES ON BODY COMPOSITION OF CATTLE BY ISOTOPE DILUTION ANALYSIS", Proc Symp. an Iso. study on physiol. of domest. Anim. IAEA/FAO, pp. 21-34, 1972. Abstract
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Lindskog, J., A. Marelius, L. G. Svensson, J. Pihl, H. Solhed, S. M. Darwish, and N. G. Jonsson, ""Electromagnetic Transition Probabilities in Nuclei"", Nucl. Phys. and Hyp. Int., Uppsala University, Progress Report (Sweden), pp. 19-25, 1972.
1973
B, W. E. N. T. W. O. R. T., M. Wineland, M. Mashaly, J. Proudman, Z. I. M. M. E. R. M. A. N, and W. Burke, "STATUS AND IMPORTANCE OF RADIOIMMUNOASSAY IN POULTRY RESEARCH", POULTRY SCIENCE, vol. 52, issue 5: POULTRY SCIENCE ASSOC INC 1111 NORTH DUNLAP AVE, SAVOY, IL 61874, pp. 2005-2005, 1973. Abstract
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Zedan, H. H., and R. Plourde, "Steroid 1-dehydrogenation and side-chain degradation enzymes in the life of cycle of Fusarium solani. ", Biochim. Biophys. Acta , vol. 326, pp. 103-115, 1973.
1974
Wentworth, B., M. Wineland, M. Mashaly, J. Proudman, N. Zimmermann, and W. Burke, "4. Status and Importance of Radioimmunoassay in Poultry Research", Poultry Science, vol. 53, issue 4: Poultry Science Association, pp. 1315-1315, 1974. Abstract
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Plourde, R., H. H. Zedan, and J. P. Lamoine, "Biotransformation de la progesterone par les spores et les cellules vegetatives de microorganismes provenant du sol Quebecois", Rev. Can. Biol. , vol. 33, pp. 111-116, 1974.
Paul, A. K., M. M. Rahman, M. M. Rahman, M. S. Islam, K. Bork, G. Witzke, J. H. Tidwell, G. Allan, R. C. Summerfelt, R. D. Clayton, et al., "Fatty acid concentration, proximate composition and mineral composition in fishbone flour of Nile Tilapia.", Journal of Fisheries and Aquatic Science, vol. 13, no. 1: orgz, pp. 40–59, 1974. Abstract
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1975
Pedersen, P., and M. M. Megahed, "Axisymmetric element analysis using analytical computing", Computers & Structures, vol. 5, no. 4: Elsevier, pp. 241–247, 1975. Abstract
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Goss, D. J., L. J. Parkhurst, and H. Görisch, "Kinetic light scattering studies on the dissociation of hemoglobin from Lumbricus terrestris.", Biochemistry, vol. 14, issue 25, pp. 5461-4, 1975 Dec 16. Abstract

The kinetics of the pH-induced dissociation of the 3 X 10(6) mol wt hemoglobin from Lumbricus terrestris (the earthworm) have been studied in a light-scattering stopped-flow apparatus. The ligand dependent dissociation data were fit well by a simple sequential model. The data for CO and oxyhemoglobin are consistent with Hb12 leads to 2Hb6 leads to 12Hb. Methemoglobin at pH 7 appears to be hexameric and the dissociation is consistent with the model: Hb6 leads to 6Hb. In a sequential decay scheme for which light-scattering changes are monitored, the relative amounts of rapid and slow phase are determined by the rate constants as well as the molecular weights of intermediate species. Assignment of the hexameric intermediate is supported by an investigation of the sensitivity of the theoretical kinetic curves to the molecular weights of the intermediates. This assignment is further supported by the following: (1) the same model will fit the data for oxy- and CO-hemoglobin at all three temperatures (a 24-29-fold variation in rate constants), (2) evidence from electron microscopy shows hexameric forms, and (3) methemoglobin is apparently stable as a hexamer at pH 7. When CO replaces O2 as the ligand, the dissociation rate increases by a factor of four. The met is about 20 times faster than the initial oxyhemoglobin dissociation rate, but perhaps more relevant for comparing dissociation of the hexamer, the met rate was respectively 100 times and 500 times faster than that for the assumed hexameric forms of CO- and oxy-hemoglobin. The activation energies for the dodecamer to hexamer dissociation and for the dissociation of the hexamer to smaller forms were about 30 kcal/mol for oxy-, CO-, and methemoglobin.

Baccanari, D., A. Phillips, S. Smith, D. Sinski, and J. Burchall, "Purification and properties of Escherichia coli dihydrofolate reductase.", Biochemistry, vol. 14, issue 24, pp. 5267-73, 1975 Dec 2. Abstract

Dihydrofolate reductase has been purified 40-fold to apparent homogeneity from a trimethoprim-resistant strain of Escherichia coli (RT 500) using a procedure that includes methotrexate affinity column chromatography. Determinations of the molecular weight of the enzyme based on its amino acid composition, sedimentation velocity, and sodium dodecyl sulfate gel electrophoresis gave values of 17680, 17470 and 18300, respectively. An aggregated form of the enzyme with a low specific activity can be separated from the monomer by gel filtration; treatment of the aggregate with mercaptoethanol or dithiothreitol results in an increase in enzymic activity and a regeneration of the monomer. Also, multiple molecular forms of the monomer have been detected by polyacrylamide gel electrophoresis. The unresolved enzyme exhibits two pH optima (pH 4.5 and pH 7.0) with dihydrofolate as a substrate. Highest activities are observed in buffers containing large organic cations. In 100 mM imidazolium chloride (pH 7), the specific activity is 47 mumol of dihydrofolate reduced per min per mg at 30 degrees. Folic acid also serves as a substrate with a single pH optimum of pH 4.5. At this pH the Km for folate is 16 muM, and the Vmax is 1/1000 of the rate observed with dihydrofolate as the substrate. Monovalent cations (Na+, K+, Rb+, and Cs+) inhibit dihydrofolate reductase; at a given ionic strength the degree of inhibition is a function of the ionic radius of the cation. Divalent cations are more potent inhibitors; the I50 of BaCl2 is 250 muM, as compared to 125 mM for KCl. Anions neither inhibit nor activate the enzyme.

Makar, A. B., K. E. McMartin, M. Palese, and T. R. Tephly, "Formate assay in body fluids: application in methanol poisoning.", Biochemical medicine, vol. 13, issue 2, pp. 117-26, 1975 Jun. Abstract
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Makar, A. B., K. E. McMartin, M. Palese, and T. R. Tephly, "Formate assay in body fluids: application in methanol poisoning.", Biochemical medicine, vol. 13, issue 2, pp. 117-26, 1975 Jun.
Makar, A. B., K. E. McMartin, M. Palese, and T. R. Tephly, "Formate assay in body fluids: application in methanol poisoning.", Biochemical medicine, vol. 13, issue 2, pp. 117-26, 1975 Jun.
Chow, Y. W., R. Pietranico, and A. Mukerji, "Studies of oxygen binding energy to hemoglobin molecule.", Biochemical and biophysical research communications, vol. 66, issue 4, pp. 1424-31, 1975 Oct 27. Abstract
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Poole-Wilson, P. A., and G. A. Langer, "Effect of pH on ionic exchange and function in rat and rabbit myocardium.", The American journal of physiology, vol. 229, issue 3, pp. 570-81, 1975 Sep. Abstract

The effects of pH variation on ionic exchange and mechanical function were studied in the arterially perfused rat and rabbit septa. The pH and PCO2 of the control perfusate were 7.40 and 39 mmHg, respectively. In the rabbit septum a metabolic acidosis (pH equals 6.82, PCO2 equals 39 mmHg) caused a loss of 16% of control tension in 12 min. Na+ and K+ exchange were unaltered. A comparable respiratory acidosis (pH equals 6.81, PCO2 equals 159 mmHg) caused a 51% loss of tension in 2 min. Na+ exchange was unaltered but K+ efflux fell from 8.9 +/- 0.6 (mean +/- SE) to 4.9 +/- 0.3 mmol/kg dry wt per min (P less than 0.001, n equals 10). A net gain of K+ of 16.9 +/- 1.7 (n equals 14) mmol/kg dry wt occurred and was attributable to a delayed fall in K+ influx relative to efflux over 15 min. The net gain could not be mimicked by epinephrine administration or blocked by propranolol and was absent in the beating rat septum and the quiescent rabbit septum. These results suggest that the net uptake of K+, which appears to be dependent on a period of depolarization, and the changes of contractility are controlled by the H+ ion concentration at a cellular site whose exchange with the extracellular space is characterized by a considerable restriction of diffusion. Changes of contractility are not related to the net uptake of K+.