| 1. |
- Fischer, S M, et al.
(författare)
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Alignment additivity in the two-quasiparticle superdeformed bands of Tl-192
- 1996
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Ingår i: Physical Review C. Nuclear Physics. - 0556-2813 .- 1089-490X. ; 53:5, s. 2126-2133
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Tidskriftsartikel (refereegranskat)abstract
- Four superdeformed bands have been confirmed in Tl-192. Two of these bands have T-(2) dynamic moments of inertia which are nearly constant with rotational frequency HBAR omega. The other two bands show the characteristic rise of T-(2) with increasing HBAR omega seen in most superdeformed bands of the A = 190 region of superdeformation. From comparisons with the odd-A neighbors, it was found that the alignments of these bands relative to a Hg-192 core can be accounted for from the additive contributions of the assigned quasiproton and quasineutron orbitals.
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| 2. |
- Humbert, F., et al.
(författare)
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Longitudinal and Transverse-Momentum Distributions of Li-9 Fragments from Break-up of Li-11
- 1995
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Ingår i: Physics Letters, Section B: Nuclear, Elementary Particle and High-Energy Physics. - 0370-2693. ; 347:3-4, s. 198-204
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Tidskriftsartikel (refereegranskat)abstract
- Transverse and longitudinal momentum distributions of Li-9 fragments from Li-11 break-up reactions in C, Al and Pb targets have been measured at 280 MeV/u. The two-neutron removal cross-section was measured to be sigma(-2n), = 0.26 +/- 0.02 b for the carbon target, sigma(-2n) = 0.47 +/- 0.08 b for the aluminum target and sigma(-2n), = 1.9 +/- 0.4 b for the lead target. No significant difference is observed between the narrow widths (FWHM approximate to 47 MeV/c) of the transverse and longitudinal momentum distributions of the Li-9 fragments. The physical implications of this are discussed.
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| 3. |
- Marques, F. M., et al.
(författare)
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Neutrons from the breakup of C-19
- 1996
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Ingår i: Physics Letters, Section B: Nuclear, Elementary Particle and High-Energy Physics. - 0370-2693. ; 381:4, s. 407-412
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Tidskriftsartikel (refereegranskat)abstract
- Neutrons arising from the breakup of a 30 MeV/nucleon C-19 beam on a tantalum target have been measured using the 98 element array DEMON. A narrow, forward peaked neutron angular distribution, with a corresponding momentum spread considerably smaller than those measured simultaneously for N-21, O-22 and F-24 was observed for charged fragments with Z
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| 4. |
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| 5. |
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| 6. |
- Mottola, S, et al.
(författare)
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The slow rotation of 253 Mathilde
- 1995
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Ingår i: PLANETARY AND SPACE SCIENCE. - : PERGAMON-ELSEVIER SCIENCE LTD. - 0032-0633. ; 43:12, s. 1609-1613
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Tidskriftsartikel (refereegranskat)abstract
- CCD photometry of the NEAR mission fly-by target 253 Mathilde is presented. Measurements taken during 52 nights of observations, from February to June 1995, allow a rotation period of 17.406 +/- 0.010 days and a lightcurve amplitude of 0.45 +/- 0.02 mag t
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| 7. |
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| 8. |
- MUELLER, MJ, et al.
(författare)
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Leukotriene A4 hydrolase: mapping of a henicosapeptide involved in mechanism-based inactivation
- 1995
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Ingår i: Proceedings of the National Academy of Sciences of the United States of America. - : Proceedings of the National Academy of Sciences. - 0027-8424. ; 92:18, s. 8383-8387
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Tidskriftsartikel (refereegranskat)abstract
- Leukotriene A4 (LTA4) hydrolase [7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9 ,11,14-tetraenoate hydrolase; EC 3.3.2.6] is a bifunctional zinc metalloenzyme which converts LTA4 into the chemotactic agent leukotriene B4 (LTB4). Suicide inactivation, a typical feature of LTA4 hydrolase/aminopeptidase, occurs via an irreversible, apparently mechanism-based, covalent binding of LTA4 to the protein in a 1:1 stoichiometry. Differential lysine-specific peptide mapping of unmodified and suicide-inactivated LTA4 hydrolase has been used to identify a henicosapeptide, encompassing the amino acid residues 365-385 of human LTA4 hydrolase, which is involved in the binding of LTA4, LTA4 methyl ester, and LTA4 ethyl ester to the native enzyme. A modified form of this peptide, generated by lysine-specific digestion of LTA4 hydrolase inactivated by LTA4 ethyl ester, could be isolated for complete Edman degradation. The sequence analysis revealed a gap at position 14, which shows that binding of the leukotriene epoxide had occurred via Tyr-378 in LTA4 hydrolase. Inactivation of the epoxide hydrolase and the aminopeptidase activity was accompanied by a proportionate modification of the peptide. Furthermore, both enzyme inactivation and peptide modification could be prevented by preincubation of LTA4 hydrolase with the competitive inhibitor bestatin, which demonstrates that the henicosapeptide contains functional elements of the active site(s). It may now be possible to clarify the molecular mechanisms underlying suicide inactivation and epoxide hydrolysis by site-directed mutagenesis combined with structural analysis of the lipid molecule, covalently bound to the peptide.
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| 9. |
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| 10. |
- Mueller, MJ, et al.
(författare)
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Leukotriene A4 hydrolase: protection from mechanism-based inactivation by mutation of tyrosine-378
- 1996
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Ingår i: Proceedings of the National Academy of Sciences of the United States of America. - : Proceedings of the National Academy of Sciences. - 0027-8424. ; 93:12, s. 5931-5935
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Tidskriftsartikel (refereegranskat)abstract
- Leukotriene A4 (LTA4) hydrolase [(7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7, 9,11,14-tetraenoate hydrolase; EC 3.3.2.6] is a bifunctional zinc metalloenzyme that catalyzes the final step in the biosynthesis of the potent chemotactic agent leukotriene B4 (LTB4). LTA4 hydrolase/aminopeptidase is suicide inactivated during catalysis via an apparently mechanism-based irreversible binding of LTA4 to the protein in a 1:1 stoichiometry. Previously, we have identified a henicosapeptide, encompassing residues Leu-365 to Lys-385 in human LTA4 hydrolase, which contains a site involved in the covalent binding of LTA4 to the native enzyme. To investigate the role of Tyr-378, a potential candidate for this binding site, we exchanged Tyr for Phe or Gln in two separate mutants. In addition, each of two adjacent and potentially reactive residues, Ser-379 and Ser-380, were exchanged for Ala. The mutated enzymes were expressed as (His)6-tagged fusion proteins in Escherichia coli, purified to apparent homogeneity, and characterized. Enzyme activity determinations and differential peptide mapping, before and after repeated exposure to LTA4, revealed that wild-type enzyme and the mutants [S379A] and [S380A]LTA4hydrolase were equally susceptible to suicide inactivation whereas the mutants in position 378 were no longer inactivated or covalently modified by LTA4. Furthermore, in [Y378F]LTA4 hydrolase, the value of kcat for epoxide hydrolysis was increased 2.5-fold over that of the wild-type enzyme. Thus, by a single-point mutation in LTA4 hydrolase, catalysis and covalent modification/inactivation have been dissociated, yielding an enzyme with increased turnover and resistance to mechanism-based inactivation.
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