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The decay modes of proton drip-line nuclei with A between 42 and 47 (1992)

Borrel, V. ; Anne, R. ; Bazin, D. ; [et al.]

Springer

The European physical journal 344 (1992), S. 135-144

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ISSN: 1434-601X

Keywords: 21.10.Dr ; 23.90.+w ; 27.40.+z

Source: Springer Online Journal Archives 1860-2000

Topics: Physics

Notes: Abstract Neutron-deficient isotopes with Z=21 to 26 have been produced as projectile-like fragments of an intense58Ni GANIL beam of 69 MeV/nucleon. The nuclei selected by the upgraded LISE3 spectrometer were identified and implanted in a silicon detector telescope. The43Cr,47Fe and46Fe isotopes were identified for the first time whereas45Fe,45Mn,44Mn and42V were not observed, indicating probable instability of these nuclei against particle emission. Measurements of the half-lives of43Cr and46Mn have been performed and the analysis of their measured beta-delayed proton spectra has given, through the isobaric multiplet mass equation, an empirical estimation of their masses. Half-lives of44Cr,43V,47Fe and46Fe have also been measured. A discussion of various mass predictions for nuclei at the proton drip-line is given.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF01291696

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Glutamylated tubulin probed in ciliates with the monoclonal antibody GT335 (1994)

Bré, Marie Hélène ; de Néchaud, Béatrice ; Wolff, Annie ; [et al.]

New York, NY : Wiley-Blackwell

Cell Motility and the Cytoskeleton 27 (1994), S. 337-349

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ISSN: 0886-1544

Keywords: microtubules ; glutamylation ; Paramecium ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Medicine

Notes: Microtubular networks are extensively developped in many ciliate species. In several of them, we investigate the occurrence of the post-translational glutamylation of tubulin [Eddé et al., 1990: Science 247:82-85; Eddé et al., 1991: J. Cell. Biochem. 46:134-142] using as a probe for such modified tubulin, the monoclonal antibody GT335 [Wolff et al., 1992: Eur. J. Cell Biol. 59:425-432]. Results obtained in Paramecium strongly suggest that both axonemal and cytoplasmic tubulin are glutamylated. As in the vertebrate brain tubulin so far tested, the GT335 epitope is located at the carboxy-terminal fragment of cytoplasmic tubulin removed by subtilisin treatment. Immunoblotting and immunofluorescence experiments reveal that, unlike tubulin acetylation, glutamylation is not restricted to cold-resistant microtubules. In addition, immunofluorescence studies performed on dividing cells show that glutamylation takes place soon after the polymerization of microtubules.Finally, glutamylated tubulin is also detected in the ciliate species Euplotes, Tetrahymena, and Paraurostyla. Together with results obtained on flagellate species, this suggests that tubulin glutamylation came out early in the course of eukaryotic evolution and has been widely exploited in various cellular strategies. © 1994 Wiley-Liss, Inc.

Additional Material: 7 Ill.