X-Ray Absorption from the Milky Way Halo and the Local Group

Million degree gas is present at near-zero redshift and is due either to a gaseous Galactic Halo or a more diffuse but very massive Local Group medium. We can discriminate between these models because the column densities should depend on location in the sky, either relative to the Galaxy bulge or to the M31-Milky Way axis. To search for these signatures, we measured the OVII Kalpha absorption line strength toward 25 bright AGNs, plus LMC X-3, using XMM-Newton RGS archival data. The data are in conflict with a purely Local Group model, but support the Galactic Halo model. The strongest correlation is between the OVII equivalent widths and the ROSAT background emission measurement in the R45 band (0.4-1 keV), for which OVII emission makes the largest single contribution. This suggests that much of the OVII emission and absorption are cospatial, from which the radius of a uniform halo appears to lie the range 15-110 kpc. The present data do not constrain the type of halo gas model and an equally good fit is obtained in a model where the gas density decreases as a power-law, such as r^(-3/2). For a uniform halo with a radius of 20 kpc, the electron density would be 9E-4 cm^(-3), and the gas mass is 4E8 Msolar. The redshift of the four highest S/N OVII measurements is consistent with a Milky Way origin rather than a Local Group origin.Comment: 32 pages (14 figures); ApJ, in pres

Equilibrium extraction characteristics of alkyl amines and nuclear fuel metals in nitrate systems: progress report for the period January 1 - September 31 [sic], 1963 : progress report XII

"December 2, 1963."Includes bibliographical references (pages 29-30)Progress report no. XII; January 1, 1963 - September 30, 1963Work performed under subcontract no. 1327 under contract no. W -7405 - Eng - 26 with Union Carbide Nuclear Corporation Oak Ridge, Tennesse

Equilibrium extraction characteristics of alkyl amines and nuclear fuel metals in nitrate systems: progress report for the period October 1 - May 30, 1964 : progress report XIII

"August 3, 1964."Includes bibliographical references (page 32)Progress report no. XIII; October 1, 1963 - May 30, 1964Work performed under subcontract no. 1327 under contract no. W -7405 - Eng - 26 with Union Carbide Nuclear Corporation Oak Ridge, Tennesse

Ditching Investigations of Dynamic Models and Effects of Design Parameters on Ditching Characteristics

Data from ditching investigations conducted at the Langley Aeronautical Laboratory with dynamic scale models of various airplanes are presented in the form of tables. The effects of design parameters on the ditching characteristics of airplanes, based on scale-model investigations and on reports of full-scale ditchings, are discussed. Various ditching aids are also discussed as a means of improving ditching behavior

ISOANTIGENS OF THE H-2 AND Tla LOCI OF THE MOUSE : INTERACTIONS AFFECTING THEIR REPRESENTATION ON THYMOCYTES

H-2 and TL isoantigens of the mouse are specified by the closely linked genetic loci H-2 and Tla. A. study of their representation on thymocytes was performed in order to reveal any interactions between the determinant genes or their products affecting the synthesis or disposition of these components of the thymocyte surface. The method employed was quantitative absorption of cytotoxic antibody by viable thymocytes. The phenotypic expression of TL antigens was found to reduce the demonstrable amount of certain H-2 antigens to as little as 34% of the quantity demonstrable on TL- thymocytes. A reduction was observed in all three H-2 types tested, (H-2b, H-2a, and H-2k). As antigenic modulation (change of TL phenotype from TL+ to TL-, produced by TL antibody) is known to entail a compensatory increase in H-2(D) antigen, it is concluded that the TL phenotype, rather than the Tla genotype, influences the surface representation of H-2 antigens. The two known TL+ phenotypes of thymocytes (TL.2 and TL.1,2,3) depress H-2 equally. The H-2 specificities affected are those determined by the D end of the E-2 locus, which is adjacent to Tla; antigens of the K end, which is distal to Tla, are not depressed. The reduction of demonstrable H-2 antigen on the thymocytes of TL+ x TL- progeny is half that of thymocytes of TL+ x TL+ progeny and the reduction affects equally the products of both H-2 alleles (cis and trans in relation to Tla), indicating that the mechanism of H-2 reduction by TL is extrachromosomal. Whether it involves diminished synthesis of H-2 or steric masking by TL at the cell membrane is unknown, but in either case the reciprocal relation of TL and H-2(D) antigens implies that they probably occupy adjacent positions on thymocytes and that the gene order, H-2(K): H-2(D):Tla is reflected in cell surface structure. Extrachromosomal interaction, apparently involving control of synthesis, occurs also within the TL system of antigens. Thymocytes of TL.2 x TL.1,2,3 progeny express the full homozygous quantity of antigens TL.1 and TL.3 (but not of TL.2), in contrast to the half-quantity present in thymocytes of TL- x TL.1,2,3 progeny. Another example of interaction is implicit in the finding that thymocytes of TL-1,2,3 x TL.1,2,3 progeny have more TL.2 antigen than thymocytes of TL.2 x TL.2 progeny, but in this instance there is nothing to indicate whether the mechanism is chromosomal or extrachromosomal. Thus the quantitative surface representation of at least some H-2 and TL antigens is influenced by the cellular complement of H-2:Tla genes as a whole. Comparison of H-2 heterozygous thymocytes with H-2 homozygous thymocytes in quantitative absorption tests shows (a) more than the expected 50% of each parental-type H-2 antigen on heterozygous cells, and (b) a greater suppression of H-2 by TL in H-2 heterozygotes in comparison with H-2 homozygotes. Both results may be explained on the basis of differences in the density of H-2 antigenic sites and consequent differences in the efficiency of absorption of H-2 antibody. These considerations may be useful in other contexts, e.g. in estimating the representation of Rh antigens on the red cells of human subjects homozygous and heterozygous for Rh components