ABSTRACT
The effects of baclofen and pancuronium bromide on evoked electromyogram (EMG), cortical electroencephalogram (EEG) and auditory brainstem responses (ABR) were studied in pentobarbital anesthetized normal rabbits. Evoked EMG was measured in the gastrocnemius muscle by electrical stimulation of the sciatic nerve. Intravenous injection of baclofen decreased EEG and arterial blood pressure and light reflex, however, it had no significant influence on EMG or ABR at doses of 10 and 20 mg/kg/h. Pancuronium bromide immediately inhibited respiration, decreased EEG and EMG, however, it had no significant influence on arterial blood pressure, ABR, or light reflex, at doses of 0.4 and 1.0 mg/kg/h in anesthetized rabbits. ABR waves were observed until just before cardiac arrest with both of the muscle relaxants. It is suggested that ABR are not influenced by central or peripheral muscle relaxants, or by pentobarbital.
Subject(s)
Baclofen/pharmacology , Electroencephalography/drug effects , Evoked Potentials, Auditory, Brain Stem/drug effects , Muscle Relaxants, Central/pharmacology , Neuromuscular Nondepolarizing Agents/pharmacology , Pancuronium/pharmacology , Acoustic Stimulation , Anesthesia , Animals , Dose-Response Relationship, Drug , Electric Stimulation , Electromyography/drug effects , Evoked Potentials/drug effects , Male , Pentobarbital/blood , Pentobarbital/pharmacokinetics , Rabbits , Reaction Time/drug effectsABSTRACT
The cDNA sequence of rabbit vitamin D-binding protein (DBP) was determined by sequencing clones isolated by immuno-screening and PCR amplification from a rabbit liver cDNA library. The 1641-nucleotide sequence included the 5' untranslated region and extended to the poly(A) tail. It encoded a protein of 460 amino acid residues in addition to a signal sequence of 16 residues, and had 84%, 79% and 78% sequence identities with human, rat and mouse DBP cDNA, respectively. In comparison with DBP amino acid sequences of other species, there are at least four heterogeneous regions. In contrast, a putative actin binding domain was conserved in the evolution process.