[Botulinum toxin and traumatic brain injury]. / Toxine botulique et traumatisme crânien.

Botulinum toxin is a successful focal spasticity therapy. The aim of this article is to study the data of the literature concerning its utilisation in traumatic brain injured patients, whom motor and tonus disturbances are polymorphic, in their clinical presentation as well as in their evolution. Although there are few studies concerning its utilisation in such patients, none of them being controlled, its use seems interesting in focal spasticity treatment. It can contribute to improve functional abilities and comfort for these patients.

Spin-5/2 Hahn echoes in solids.

The Hahn echoes for a spin I = 5/2 system were derived by considering the first-order quadrupole interaction throughout the experiment. Consequently, our results are valid for any ratio of the quadrupole coupling, omega Q, to the amplitude of the RF pulse, omega RF. The use of simplified density operators reduced the computation time dramatically. Furthermore, this approach allows a better understanding of the origin of the Hahn echoes in half-integer quadrupole spins. The tau 4 = tau 2 Hahn echoes were illustrated with the 27Al nucleus in a polycrystalline sample of KAl(SO4)2.12H2O. The quadrupole coupling constant and the asymmetry parameter of 27Al were determined by two methods: from the lineshape of the powder pattern and from the variation of the central line integrated intensity as a function of the second pulse duration.

In vitro translation of poliovirus RNA: utilization of internal initiation sites in reticulocyte lysate.

The translation of poliovirus RNA in rabbit reticulocyte lysate was examined. Translation of poliovirus RNA in this cell-free system resulted in an electrophoretic profile of poliovirus-specific proteins distinct from that observed in vivo or after translation in poliovirus-infected HeLa cell extract. A group of proteins derived from the P3 region of the polyprotein was identified by immunoprecipitation, time course, and N-formyl-[35S]methionine labeling studies to be the product of the initiation of protein synthesis at an internal site(s) located within the 3'-proximal RNA sequences. Utilization of this internal initiation site(s) on poliovirus RNA was abolished when reticulocyte lysate was supplemented with poliovirus-infected HeLa cell extract. Authentic P1-1a was also synthesized in reticulocyte lysate, indicating that correct 5'-proximal initiation of translation occurs in that system. We conclude that the deficiency of a component(s) of the reticulocyte lysate necessary for 5'-proximal initiation of poliovirus protein synthesis resulted in the ability of ribosomes to initiate translation on internal sequences. This aberrant initiation could be corrected by factors present in the HeLa cell extract. Apparently, under certain conditions, ribosomes are capable of recognizing internal sequences as authentic initiation sites.

Monoclonal antibodies which recognize native and denatured forms of the adenovirus DNA-binding protein.

Two hybridoma cell lines were obtained, A1 and B6, which produced monoclonal antibodies reacting with the 44,000-MW C-terminal domain of the adenovirus type 5 DNA-binding protein (DBP). Clone A1 antibodies reacted with the native form of the DBP, but failed to recognize this protein after denaturation (by exposure to sodium dodecylsulfate, or production of the DBP at 39.5 degrees by H5ts107, a temperature-sensitive DBP mutant). Clone B6 antibodies bound to both the native and denatured forms of the DBP. Immunofluorescent staining of wild-type-virus infected cells revealed the DBP located in discrete nuclear patches. A1 and B6 antibodies detected this patched localization of the DBP in nuclei of H5ts107-infected cells grown at 32 degrees. However, at the nonpermissive temperature of 39.5 degrees, A1 antibodies failed to detect the DBP, and B6 antibodies gave a uniform nuclear fluorescent distribution of the DBP. Thus the nuclear pattern of localization for the DBP synthesized by H5ts107 was temperature dependent in this mutant.