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2.
Anaesthesiol Reanim ; 18(5): 120-2, 125-7, 1993.
Article in German | MEDLINE | ID: mdl-8280339

ABSTRACT

Central, peripheral and cardiac side-effects of both anticholinergic drugs atropine and glycopyrrolate were compared during the antagonism of muscle relaxation with pyridostigmine. In a randomized, double-blind fashion 50 patients were given 10 micrograms/kg of atropine and 50 were given 5 micrograms/kg of glycopyrrolate with 125 micrograms/kg pyridostigmine intravenously. Continuous Holter ECG-monitoring over 3 hours was performed. The procedure was divided into the following phases: control (5 minutes before application of antagonists), phase I (application of antagonists and the following 5 minutes), phase II (subsequent 30 minutes), phase III (until 3 hours had passed). The first 32 minutes were subdivided into periods of 4 minutes. Analysed were: 1st: The number of patients with supraventricular, junctional and ventricular beats, 2nd: The mean heart rate per period, 3rd: The incidence of central-anticholinergic syndromes and the peripheral antimuscarinic side-effects. Supraventricular beats were found after atropine in 42 patients and after glycopyrrolate in 18 patients (p < 0.001). The differences mainly occurred during phase I (atropine 15 vs. glycopyrrolate 4 p < 0.05) and III (atropine 38 vs. glycopyrrolate 18, p < 0.01). Junctional beats were found after both drugs (atropine 7 vs. glycopyrrolate 10), above all during phase III. Ventricular beats were observed after atropine (21) and glycopyrrolate (18). Atropine as well as glycopyrrolate caused an increased heart rate within the first 4 minutes (atropine 47% vs. glycopyrrolate 27%, p < 0.01). During phase III after atropine, the heart rate decreased below the control value (p < 0.05). None of the patients showed central anticholinergic syndromes after either drug.(ABSTRACT TRUNCATED AT 250 WORDS)


Subject(s)
Atropine/adverse effects , Glycopyrrolate/adverse effects , Heart/drug effects , Muscle Relaxation/drug effects , Pyridostigmine Bromide/pharmacology , Adult , Aged , Arrhythmias, Cardiac/chemically induced , Arrhythmias, Cardiac/epidemiology , Atropine/administration & dosage , Double-Blind Method , Female , Glycopyrrolate/administration & dosage , Heart Rate/drug effects , Humans , Injections, Intravenous , Male , Middle Aged
3.
Arch Microbiol ; 150(6): 564-6, 1988.
Article in English | MEDLINE | ID: mdl-3144958

ABSTRACT

In Bacillus subtilis, heat shock proteins can be classified into two main groups: specific heat shock proteins (about 5) and general stress proteins (at least 14). Salt stress was very effective in the induction of general stress proteins (5 to 50-fold stimulation), but the synthesis of heat-specific stress proteins was not stimulated. Furthermore there were some proteins whose synthesis was accelerated only by salt stress.


Subject(s)
Bacillus subtilis/metabolism , Bacterial Proteins/biosynthesis , Heat-Shock Proteins/biosynthesis , Sodium Chloride , Bacterial Proteins/classification , Bacterial Proteins/isolation & purification , Heat-Shock Proteins/classification , Heat-Shock Proteins/isolation & purification , Hot Temperature , Osmotic Pressure
4.
Z Naturforsch C J Biosci ; 42(7-8): 941-7, 1987.
Article in German | MEDLINE | ID: mdl-2961154

ABSTRACT

Some of the presumable heat shock proteins will be produced in Bacillus subtilis in response to different environmental conditions, e.g. heat shock, amino acid limitation or oxygen limitation. During amino acid limitation or during oxygen limitation the relA+ strain is able of synthesizing this set of proteins but the relA strain is not. We suggest that the accelerated rate of the synthesis of some heat shock proteins depends on the induction of the stringent response because the (p)ppGpp production does not occur in the relA strain during amino acid or oxygen limitation. On the other hand the relA strain can produce heat shock proteins under heat stress. Therefore different mechanisms must be responsible for the expression of this set of genes during heat and other stress stimuli. It can be supposed that in B. subtilis the (p)ppGpp-dependent stringent control is a central defense reaction against different adverse environmental conditions and furthermore, that the synthesis of "stress" proteins as an essential component of the stringent response is part of a general adaptation mechanism under non-growing conditions.


Subject(s)
Amino Acids/metabolism , Bacillus subtilis/metabolism , Heat-Shock Proteins/biosynthesis , Oxygen/pharmacology , Bacillus subtilis/drug effects , Bacillus subtilis/genetics , Heat-Shock Proteins/isolation & purification , Kinetics , Species Specificity
5.
Zentralbl Mikrobiol ; 140(8): 631-9, 1985.
Article in German | MEDLINE | ID: mdl-3938143

ABSTRACT

Growing cultures of Pseudomonas aeruginosa and Bacillus megaterium show after treatment with cetyltrimethylammonium bromide (CTAB) typical concentration-dependent alterations of envelope. In Ps. aeruginosa low doses of the detergent cause perforations and lesions of the cytoplasmic membrane, by 0.016% CTAB the formation of extracellular vesicles of the outer membrane ("blebs") and the intracellular assembly of lamellar structures can be detected. These intracellular lamellar structures are artifacts of the cytoplasmic membrane after detergent application. In this case the conglomeration of bacterial cells can be demonstrated with the scanning electron microscope. The results are discussed in connection with the use of CTAB in inactivation and permeabilization of bacteria.


Subject(s)
Anti-Infective Agents, Local/pharmacology , Bacillus megaterium/drug effects , Cetrimonium Compounds/pharmacology , Pseudomonas aeruginosa/drug effects , Quaternary Ammonium Compounds/pharmacology , Cell Membrane/drug effects , Cell Membrane Permeability/drug effects , Cetrimonium , Dose-Response Relationship, Drug
6.
Z Allg Mikrobiol ; 22(1): 69-71, 1982.
Article in English | MEDLINE | ID: mdl-6803450

ABSTRACT

The application of a protamine-ferritin conjugate for labelling of isolated protoplast membranes of Bacillus subtilis S 13/1 is described. Contrary to Mycoplasma membranes which could only be labelled on the outer side of the membrane, ferritin was deposited on both membrane sides as a single layer without cluster formation.


Subject(s)
Bacillus subtilis/analysis , Bacillus subtilis/ultrastructure , Cell Membrane/analysis , Ferritins/metabolism , Polymers/metabolism , Protamines , Protoplasts/analysis , Surface Properties
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