High-current hollow-cathode source as a radiant intensity standard in the 40-125-nm wavelength range.
The radiant intensity of VUV emission lines of a high-current hollow-cathode source has been determined for the 40-125-nm spectral range. The source is operated at a constant current of 1 A with an aluminum cathode. Different rare gases are alternatively used as the buffer gas at pressures of ~100 Pa. The radiant intensity has been determined by comparison with the calculable spectral radiant flux of the electron storage ring BESSY. Radiant intensities of the emission lines are in the 7-1400-µW/sr range. The long-term reproducibility of the radiant intensity of the source is within ±10% (2σ value). The systematic uncertainty of the radiometric calibration is better than 9% (√32σ value).
Electron-atom source as a primary radiometric standard for the EUV spectral region.
A compact, portable radiometric standard for the EUV wavelength region utilizing single photon counting is described. An energetic beam of electrons is passed through a thin atomic or molecular gas target inducing radiative transitions. The absolute flux of radiation per unit length of beam emitted in a spectral line can be calculated from the current of electrons and the number density of the target gas if the relevant electronimpact photoemission cross section is known at the electron-impact energy used. In typical operating conditions and for a photoemission cross section of 10(-22) m(2), the emitted flux of photons can be 10(10) photons/s/cm of beam length resulting in a count rate of 500 counts/s into an f/6 spectrometer-detector system. Assessment of previously measured electron-impact photoemission cross sections indicates that, once precision benchmark cross-sectional measurements are available, ultimate uncertainties as low as 3% could be obtained for this standard.
Cytoplsmic uridine phosphorylase of rat liver. Characterization and kinetics.
Abstract Uridine phosphorylase (uridine:orthophosphate ribosyltransferase, EC 2.4.2.3) of rat liver cytoplasm has been purified 1900-fold. Initial velocity patterns of the phosphorolysis of uridine or deoxyuridine and of the synthesis of uridine indicated a sequential mechanism. Product inhibition patterns with uracil or ribose 1-phosphate as inhibitors were consistent with an "ordered Bi Bi" reaction in which inorganic phosphate is the first substrate to bind to the enzyme and ribose 1-phosphate the last product to leave the enzyme. The most highly purified enzyme fractions still retained uridine-, deoxyuridine-, and thymidine-cleaving activities in the ratio of 10:7:1 at pH 7.4. The fractions separated into a major and a minor band of protein on electrophoresis in phosphate buffer. Aging of the enzyme with loss of activity resulted in an increase in the proportion of the minor band. The pH optimum of the enzyme for uridine cleavage was 8.2, for deoxyuridine cleavage, 6.5, and for uridine synthesis, 8.5. Uridine or deoxyuridine synthesis was inhibited 50% in the presence of 1 mm uracil. The enzyme did not catalyze the direct transfer of ribose from uridine to uracil in the absence of phosphate. Uridine protected the enzyme to a greater degree than phosphate against inhibition by o-iodosobenzoate. Thus, at least one sulfhydryl group and possibly three are present at or near the active site. Uridine cleavage, uridine synthesis, and deoxyuridine cleavage were inhibited by deoxyglucosylthymine. The phosphorolysis of deoxyuridine and thymidine by thymidine phosphorylase, also purified from rat liver cytoplasm, was not inhibited by deoxyglucosylthymine. The molecular weights of both uridine and thymidine phosphorylases were estimated to be 110,000.