Psychiatric diseases and their treatment in general practice in Germany. Results of a World Health Organization (WHO) study

As part of an international study initiated by the World Health Organization (WHO) about psychological disorders in primary health care, patients in the Federal Republic of Germany were compared with patients in other European centres. Patients from Germany do not differ from other European patients in respect to sociodemographic variables or psychiatric disorders. The most frequent CIDI-based diagnoses recorded in patients attending general practices are current depressive episodes (8.6%), generalized anxiety disorders (8.5%), neurasthenia (7.5%), and alcohol dependence (6.3%). In 20.9% of the patients at least one psychiatric diagnosis based on ICD-10 was recorded. In Germany significantly lower global ratings of health status are given than in other European centres although there is no difference in diagnostic prevalence rates. The recognition rate, i.e. the agreement between the CIDI-based ICD-10 diagnoses and the recognition as a case by the physician, is 56.2%-60.2%. On the other hand, the CIDI detects 90% of the patients described as psychologically ill by the physicians if subthreshold cases are also counted, or 46.4% if only defined diagnoses are taken into account. There is a significant correlation between severity of the psychiatric disorder and disability in social functioning. In Mainz and in the other European countries the disability rate of patients with a well-defined disorder is between 67.0% and 72.7%, whereas in Berlin this relation is not as clear, because especially in East Berlin there is a higher rate of unemployment in view of the political situation. Drug treatment is prescribed for 16.1% of the patients in primary care for psychiatric disorders. Half the patients recognized by physicians as cases receive medication. In the rest of Europe patients receive significantly more tranquillizers than in Germany, where the use of herbal drugs is more wide spread.     

Isolation and enzymatic fragmentation of the coeliac-active gliadin peptide CT-1

Summary Investigations on the structure/toxicity relationships of gliadin peptides were continued with the coeliac-active gliadin peptide CT-1, which is derived from the N-terminal portion (residues 3–24 of the amino acid sequence) of-gliadins [this journal (1986) 182:115–117]. CT-1 was produced by chymotryptic digestion and reversed-phase (RP) HPLC from the peptide fraction G3 [this journal (1992) 194:1–6] and digested with the proteases endoproteinase Glu-C, pancreatin, papain and thermolysin. The fragment peptids were separated by preparative RP-HPLC and characterized by amino acid analysis. On the basis of the specifity of the enzymes for CT-1 and the toxic effect of enzymatic hydrolysates of gliadin described in the literature, the significance of partial sequences, in particular of the sequence -Pro-Ser-Gln-Gln-Gln-Pro- for the coeliac-toxicity effect, is discussed.

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Isolierung und enzymatische Fragmentierung des coeliakieaktiven Gliadinpeptids CT-1

Zusammenfassung Die Untersuchungen über die Zusammenhänge zwischen der Struktur von Gliadinpeptiden und ihrer Toxizität wurden mit dem coeliakieaktiven Gliadinpeptid CT-1 fortgesetzt, das aus dem N-terminalen Bereich (Positionen 3–24 der Aminosäuresequenz) von-Gliadinen stammt [diese Zeitschrift (1986) 182:115–117]. CT-1 wurde aus der Peptidfraktion G3 [diese Zeitschrift (1992) 194:1–6] durch chymotryptische Partialhydrolyse und Umkehrphasen-HPLC gewonnen und mit den Proteasen Endoproteinase Glu-C, Pankreatin, Papain und Thermolysin umgesetzt. Die entstandenen Fragmentpeptide wurden durch präparative Umkehrphasen-HPLC getrennt und durch Aminosäurenanalyse charakterisiert. Anhand der Spezifität der Enzyme gegenüber CT-1 und der aus der Literatur bekannten toxischen Wirkung von enzymatischen Gliadinhydrolysaten wird die Bedeutung einzelner Sequenzabschnitte, insbesondere der Sequenz-Pro-Ser-Gln-Gln-Gln-Pro-, für die coeliakiespezifische Wirkung diskutiert.

     

Coeliac activity of the gliadin peptides CT-1 and CT-2

Summary The coeliac active peptide B 3142, which has been isolated from a peptic-tryptic digest of gliadin [1] and which consists of 53 amino-acid sequences [2], was partially hydrolyzed with -chymotrypsin. The two fragment peptides CT-1 (positions 1–22 of B 3142) and CT-2 (positions 23–53) were separated by high-performance liquid chromatography on octadecyl silica gel and purified by gel filtration on Biogel P2. The examination in the organ-culture test including 18 coeliac patients on normal diet and 7 control persons have shown that the toxicity is preserved after the chymotryptic treatment and that the peptides B 3142, CT-1 and CT-2 do not significantly differ from one another according to their coeliac-specific effect.

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Coeliakieaktivitat der Gliadinpeptide CT-1 und CT-2

Zusammenfassung Das coeliakieaktive Peptid B 3142, das aus einem peptisch-tryptischen Partialhydrolysat von Gliadin gewonnen wurde [1] und aus einer Sequenz von 53 Aminosäureresten besteht [2], wurde mit -Chymotrypsin partiell hydrolysiert. Die beiden Fragment-peptide CT-1 (Positionen 1–22 von B 3142) und CT-2 (Positionen 23–53) wurden durch Hochdruckflüssig-keitschromatographie an Octadecyl-Kieselgel aufgetrennt und an Biogel P2 gereinigt. Die Prüfung im Organkultur-Test unter Einbeziehung von 18 Coeliakie-patienten unter Normalkost und von 7 Kontrollpersonen zeigte, daß die Toxizität nach chymotryptischer Spaltung erhalten bleibt, und daß sich die Peptide B 3142, CT-1 und CT-2 in ihrer coeliakiespezifischen Wirkung nicht wesentlich unterscheiden.

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Supported by a grant from Deutsche Forschungsgemeinschaft. We gratefully acknowledge the excellent assistance given by Mrs. U. Schützler and Ms. B. Mosler     

Microscopical studies of water/flour systems

Summary Wheat flour particles sprinkled on a water surface form strands which are visible in the light microscope. These strands form aggregates by means of mechanical forces which show viscoelastic behaviour. Amino acid analysis of both the protein strands and the aggregates formed shows that they consist of gluten protein. The formation of the protein strands occurs at the air/water interface and results from the action of a protein film which spreads around the flour particles.

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Mikroskopische Untersuchungen von Mehl/Wasser-Systemen

Zusammenfassung Weizenmehlpartikel, die auf Wasser gestreut werden, bilden lichtmikroskopisch sichtbare Stränge aus. Durch mechanische Beanspruchung lassen sich these Stränge zu Aggregaten zusammenfassen, die visco-elastisches Verhalten zeigen. Die Aminosäureanalyse sowohl der Proteinstrange wie auch der daraus gebildeten Aggregate zeigt, daß es sich dabei um Kleberprotein handelt. Die Proteinfäden entstehen an der Wasser-Luft-Grenzflache als Folge eines spreitenden Proteinfilms, der sich um die Mehlpartikel herum ausbreitet.

     

Trypsin-/Chymotrypsin-Inhibitoren in Samen der Puffbohne (Vicia faba)

Zusammenfassung Durch isoelektrisches Fokussieren wurden mehrere Trypsin/Chymotrypsin-Inhibitoren in Samen vonVicia faba nachgewiesen, deren isoelektrische Punkte bei pH 8,5 (Hauptpeak mit Schulter) und bei pH 9,1 (Nebenpeak mit Schulter) sowie im Bereich von pH 9,1-6,4 (Nebenpeaks mit deutlich geringeren Aktivitäten) liegen. Aus einem durch Affinitätschromatographie an trägergebundenem Trypsin erhaltenen Inhibitorgemisch wurden drei Inhibitoren durch preparative Elektrophorese in Polyacrylamidgel isoliert, die sich bei pH 9,2 und bei pH 4,0 als elektrophoretisch einheitlich erwiesen. Die Molekulargewichte liegen bei 6000 Dalton. Der Anteil an basischen Aminosäuren ist hoch, während Methionin und Isoleucin fehlen. Die Hemmwirkung ist spezifisch auf Serinproteinasen gerichtet: Neben Trypsin und Chymotrypsin werden einige mikrobielle Enzyme dieser Gruppe gehemmt. Die thermische Stabilität ist relativ groß. Die Inhibitoren ausVicia unterscheiden sich damit in einer Reihe von Eigenschaften deutlich von den Inhibitoren ausPhaseolus.

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Inhibitors for trypsin and chymotrypsin in seeds of the broad bean (Vicia faba)

Summary Several inhibitors for trypsin and chymotrypsin were detected in seeds ofVicia faba by isoelectric focussing. Their isoelectric points are at pH 8.5 (main peak with shoulder), at pH 9.1 (minor peak with shoulder) and in the range of pH 9.1-6.4 (several minor peaks with significant lower activities). From the mixture of inhibitors obtained by affinity chromatography on carrier bound trypsin, three inhibitors were isolated by preparative electrophoresis in polyacrylamide gel. On electrophoresis these inhibitors behaved uniformly at pH 9.2 and at pH 4.0. Their molecular weights are about 6000 daltons. The amount of basic amino acids is high, while methionine and isoleucine are absent. Besides of trypsin and chymotrypsin some serine proteinases of microbial origin are inhibited. The thermal stability is quite high. TheVicia inhibitors therefore differ significantly from thePhaseolus inhibitors in several properties.

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Der AIF und dern Forschungskreis der Ernährungsindustrie danken wir für die finanzielle Unterstützung     

CMOS and SiGe bipolar circuits for applications up to 110 GHz

Recently, CMOS has been demonstrated to be a viable technology for very-high-bit-rate broad-band and wireless communication systems up to 40 Gb/s and 50 GHz. Advances in device scaling and doping-profile optimization have also resulted in SiGe bipolar transistors with impressive performance, including cut-off frequencies of more than 200 GHz. This paper presents advances in circuit design which fully exploit the high-speed potential of a 0.13 µm CMOS technology up to 50 GHz and of a high-performance SiGe bipolar technology up to 110 GHz operating frequency. The combination of advanced circuit techniques and a state-of-the-art fabrication-process technology results in continuing the upward shift of the frequency limits.