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N Andorn

Publications and source records attributed to N Andorn.

5 recordsLinked to original sources

Radiation-induced generation of chlorine derivatives in N2O-saturated phosphate buffered saline: toxic effects on Escherichia coli cells.

The radiolysis of aqueous chloride solutions has been investigated using pulse and steady-state methods. We have found a correlation between the yields of Cl2- and HOCl formed in pulse-irradiated N2O-saturated solutions. The yields increased with the increasing concentrations of Cl- and phosphate. Phosphate enhanced the yield of Cl2- in neutral solutions because of a proton transfer from H2PO4- to HOCl- with a rate constant of (2.6 +/- 0.5) x 10(8) M-1s-1. HOCl could not be detected in pulse-irradiated He or air-saturated, phosphate-buffered saline (PBS) solutions or in gamma-irradiated N2O, He, or air-saturated PBS solutions. The results are discussed in light of previously suggested mechanisms for the formation and decay of Cl2-. Pulse-irradiated N2O-saturated PBS solutions have a lethal effect on Escherichia coli cells, which is proportional to the amount of HOCl in the solutions. Gamma-irradiation of cells in N2O-saturated PBS solution also raises the radiosensitivity of the cells, although HOCl does not accumulate in this system. The effects of the radiation-induced toxic products on E. coli cells are similar to the effects of NaOCl. The cell membrane is probably the site of physiological injury induced by the radiation products.

Adenosine Triphosphate

Immunoadsorption of histidinol dehydrogenase in the presence of urea.

Urea inhibits the activity of histidinol dehydrogenase from Escherichia coli B, prevents precipitation of the enzyme by specific antibodies and dissolves immunoprecipitates which were formed in the absence of urea. However, immunoadsorption of the enzyme to Sepharose-bound antibodies can take place in the presence of high concentrations (5-8 M) of urea. The immobilized antibody-bound enzyme exhibits almost full activity after removal of the urea and is inhibited by soluble specific antibodies in the presence of urea. The possibility of using immunoadsorption in the presence of urea for the study of insoluble proteins is discussed.

Alcohol Oxidoreductases

Purification and properties of histidinol dehydrogenase from Escherichia coli B.

Histidinol dehydrogenase has been purified from a derepressed mutant of Escherichia coli B. A molecular weight of about 91,000 was estimated by gel filtration. The native enzyme seems to be composed of two similar subunits which have a molecular weight of 52,000 as determined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The pI of the enzyme as determined by isoelectric focusing is 4.75. The enzyme is maximally active at pH 9.5. It is highly specific for NAD+ and histidinol, with a Km (NAD+) of 0.57 mM and a Km (histidinol) of 14 microM. Mn2+ is required for maximal activity. The enzyme is completely inactivated by 8 M-urea but regains its activity very quickly upon removal of the urea. Mn2+ and histidinol protect the enzyme from heat inactivation.

Alcohol Oxidoreductases