Efficacy and tolerability of valerian extract LI 156 compared with oxazepam in the treatment of non-organic insomnia--a randomized, double-blind, comparative clinical study.

Patients aged 18 to 73 years and diagnosed with non-organic insomnia according to ICD-10 (F 51.0) were treated in a multicentre, double-blind, randomised parallel group comparison with either 600 mg/die valerian extract LI 156 (Sedonium) or 10 mg/die oxazepam taken for 6 weeks. A total of 202 outpatients with a mean duration of insomnia of 3.5 months at baseline were included at 24 study centres (general practices) in Germany. - Sleep quality (SQ) after 6 weeks measured by the Sleep Questionnaire B (SF-B; CIPS 1996) showed that 600 mg/die valerian extract LI 156 was at least as efficacious as a treatment with 10 mg/die oxazepam. Both treatments markedly increased sleep quality compared with baseline (p <0.01). The other SF-B subscales, i.e. feeling of refreshment after sleep (GES), psychic stability in the evening (PSYA), psychic exhaustion in the evening (PSYE), psychosomatic symptoms in the sleep phase (PSS), dream recall (TRME), and duration of sleep confirmed similar effects of both treatments. Clinical Global Impressions scale (CGI) and Global Assessment of Efficacy by investigator and patient, again, showed similar effects of both treatments. Adverse events occurred in 29 patients (28.4%) receiving valerian extract LI 156 and 36 patients (36.0%) under oxazepam, and were all rated mild to moderate. No serious adverse drug reactions were reported in either group. Most patients assessed their respective treatment as very good (82.8% in the valerian group, 73.4% in the oxazepam group). During the 6 week treatment phase Valerian extract LI 156 (Sedonium) 600 mg/die showed a comparable efficacy to 10 mg/die oxazepam in the therapy of non-organic insomnia.

The N-terminal amino acid sequences of the Plasmodium falciparum (FCB1) merozoite surface antigens of 42 and 36 kilodalton, both derived from the 185-195-kilodalton precursor.

The N-terminal amino acid sequences of the 42- and 36-kDa Plasmodium falciparum (strain FCB1) merozoite surface polypeptides, both processing fragments from the 185-195-kDa polymorphic glycoprotein, have been obtained. The N-terminus of the 42-kDa fragment is located in the amino acid sequence of the precursor molecule at amino acid residue 1255 (numbering according to Mackay, M., Goman, M., Bone, N., Hyde, J.E., Scaife, J., Certa, U., Stunnenberg, H. and Bujard, H. (1985) EMBO J. 4, 3823-3829). The peptide bond cleaved during processing is Glu-Ala. This fragment is derived from the C-terminal end of the precursor molecule. The N-terminus of the 36-kDa fragment is located in the precursor molecule at amino acid residue 902 (numbering as above), and the bond cleaved is Asn-Asp.

A 46,000 dalton Plasmodium falciparum merozoite surface glycoprotein not related to the 185,000-195,000 dalton schizont precursor molecule: isolation and characterization.

A 46,000 dalton glycoprotein was isolated by extraction of freshly harvested P. falciparum merozoites (FCB1 strain), followed by gel electrophoresis of the extract and electroelution. The antigen is present in the late ring, trophozoite, schizont, and segmenter stages and is localized on the merozoite surface at the end of schizogony. It is not related to the 185,000-195,000 dalton schizont antigen. An antiserum against the 46,000 dalton antigen inhibits invasion of erythrocytes by merozoites. The isolated antigen is identical to the antigen against which monoclonal antibody (mcab) 13.4 is directed.

Isolation and characterization of the 80,000 dalton Plasmodium falciparum merozoite surface antigen.

The 80,000 dalton merozoite surface protein, derived from the 185,000-195,000 dalton schizont precursor, was isolated from detergent extracts of naturally-released merozoites using chromatographic procedures. A rabbit antiserum raised against this antigen was used for characterizing the 80,000 dalton fragment. The antiserum did not inhibit merozoite invasion or parasite growth in vitro, suggesting that this merozoite surface antigen is not directly involved in the invasion process of the merozoite into the host erythrocyte.