Der Sperlingskauz (Glaucidium passerinum) im Schwarzwald

Summary After a decrease and extinction due to deforestation the population has been reestablished by releasing captive-bred owls. Now about 40 territories are occupied with an average density of 0,8–1,0 territories/10 km². Highest density: 17 territories/80 km².     

Human inter-alpha-trypsin inhibitor: localization of the Kunitz-type domains in the N-terminal part of the molecule and their release by a trypsin-like proteinase

The N-terminal amino-acid sequence of human ITI has been found to be identical with that of the acid-stable human 30-kDa inhibitors (HI-30) from urine, serum, and those released from inter-alpha-trypsin inhibitor by trypsin or chymotrypsin. Serum HI-30 and HI-30 released by trypsin differ from the urinary inhibitor by an additional C-terminal arginine residue. Compared to these two inhibitors the inhibitor released by chymotryptic proteolysis is elongated C-terminally by an additional phenylalanine residue. These results strongly favour HI-30 as the N-terminus of the inter-alpha-trypsin inhibitor and its release from this inhibitor in vivo by cleavage of the Arg123-Phe124 peptide bond by trypsin-like proteinases.     

Isolation of acid-resistant urinary trypsin inhibitors by high performance liquid chromatography and their characterization by N-terminal amino-acid sequence determination

Two crude fractions of acid-resistant trypsin inhibitors (apparent molecular masses 44 and 20 kDa, respectively) were prepared from human urine by gel permeation chromatography. From both preparations the pure inhibitors were isolated by high performance liquid chromatography (HPLC). Their N-terminal amino-acid sequences were determined and compared with those of HI-30 and HI-14 as isolated by reversible binding to either immobilized trypsin or immobilized chymotrypsin. The N-terminal amino-acid sequence of the high-molecular mass inhibitor UI-I isolated by HPLC was identical with those of HI-30 and UI-C-I isolated via immobilized trypsin or chymotrypsin, respectively. The low-molecular mass inhibitors UI-II and UI-C-II differ from HI-14 by the N-terminal extension Glu-Val-Thr-Lys-when obtained by HPLC or by the extension Thr-Lys-when obtained via immobilized chymotrypsin, respectively. The comparison of these N-termini with the amino-acid sequence of HI-30 (Ala1-...-Val16-Thr-Glu-Val-Thr-Lys-HI-14) defines the low molecular urinary trypsin inhibitors as proteolytic degradation products of the high-molecular urinary inhibitor. Proteolysis may occur at different bonds. The existing discrepancies in molecular architecture and in molecular masses of the urinary trypsin inhibitors are discussed.     

Enterohepatic circulation of N-acetyl-leukotriene E4

N-Acetyl-leukotriene E₄, the end product of leukotriene C₄ metabolism in the mercapturic acid pathway, was rapidly eliminated from the blood circulation into the bile of rats. Part of the N-acethyl-leukotriene E₄ secreted from bile into the intestine undewent enterohepatic circulation. Leukotriene absorption occurred from the small intestine and from the colon. Biliary and urinary excretion within 5.5 h amounted to 15 and 2%, respectively, of the intraduodenally administered N-acetyl- H leukotriene E₄ in animals anesthetized with ketamine. HPLC analyses indicated that 35% of the biliary radioactivity corresponded to unchanged N-acetyl- H leukotriene E₄, while 65% in bile and 100% in urine were polar metabolites. Enterohepatic circulation extends the biological half-life of N-acetyl-leukotriene E₄.     

Prostaglandin 12 reduces activation of human arterial smooth muscle cells in-vivo

Patients suffering from peripheral vascular disease have been “ultima ratio”-treated with PGI2 at a rate of 5 ng/kg/min for 6 hours a day and 5 consecutive days i.v. 20 of them underwent surgery thereafter as therapy was not sufficient. A histological examination and quantification of vascular tissue revealed that the number of activated smooth muscle cells was significantly lower in treated patients vascular segments than in untreated ones in all the different age groups. A comparable suppression was found in the intima and the media as well. It is thus concluded, that PGI2 inhibits smooth muscle cell proliferation most probably by inhibiting PDGF-release from the platelets and stimulation of smooth muscle cell cAMP. To achieve a more beneficial PGI2-effect at the vascular level, a prolonged PGI2-therapy looks rather promising.     

Analysis of the energy metabolism after incubation of Saccharomyces cerevisiae with sulfite or nitrite

After addition of 5 mM sulfite or nitrite to glucose-metabolizing cells of Saccharomyces cerevisiae a rapid decrease of the ATP content and an inversely proportional increase in the level of inorganic phosphate was observed. The concentration of ADP shows only small and transient changes. Cells of the yeast mutant pet 936, lacking mitochondrial F₁ATPase, after addition of 5 mM sulfite or nitrite exhibit changes in ATP, ADP and inorganic phosphate very similar to those observed in wild type cells. They key enzyme of glucose degradation, glyceraldehyde-3-phosphate dehydrogenase was previously shown to be the most sulfiteor nitrite-sensitive enzyme of the glycolytic pathway. This enzyme shows the same sensitivity to sulfite or nitrite in cells of the mutant pet 936 as in wild type cells. It is concluded that the effects of sulfite or nitrite on ATP, ADP and inorganic phosphate are the result of inhibition of glyceraldehyde-3-phosphate dehydrogenase and not of inhibition of phosphorylation processes in the mitochondria. Levels of GTP, UTP and CTP show parallel changes to ATP. This is explained by the presence of very active nucleoside monophosphate kinases which cause a rapid exchange between the nucleoside phosphates. The effects of the sudden inhibition of glucose degradation by sulfite or nitrite on levels of ATP, ADP and inorganic phosphate are discussed in terms of the theory of Lynen (1942) on compensating phosphorylation and dephosphorylation in steady state glucose metabolizing yeast.Abbreviations ATP adenosine triphosphate - ADP adenosine diphosphate - AMP adenosine monophosphate - P_i inorganic orthophosphate Dedicated to Prof. Dr. Hans Grisebach on the occasion of his sixtieth birthday     

Thermotoga maritima sp. nov. represents a new genus of unique extremely thermophilic eubacteria growing up to 90°C

A novel type of bacterium has been isolated from various geothermally heated locales on the sea floor. The organisms are strictly anaerobic, rod-shaped, fermentative, extremely thermophilic and grow between 55 and 90°C with an optimum of around 80°C. Cells show a unique sheath-like structure and monotrichous flagellation. By 16S rRNA sequencing they clearly belong to the eubacteria, although no close relationship to any known group could be detected. The majority of their lipids appear to be unique in structure among the eubacteria. Isolate MSB8 is described as Thermotoga maritima, representing the new genus Thermotoga.Dedicated to Otto Kandler on the occasion of his 65th birthday Present addresses: University of South Dakota, Vermillion, USA; University of Illinois, Urbana, USA; Universität für Bodenkultur, Wien, Austria     

Cytochrome c oxidase. Time dependence of optical and EPR spectral changes related to the ‘oxygen-pulsed’ form

Time-dependent changes in the optical spectrum (450–920 nm) of cytochrome c oxidase, following oxidation with oxygen of the stoichiometrically reduced form, have been investigated and where possible, attempts have been made to correlate our observations with variations in the EPR spectrum over a parallel time course at 2°C. In this regard, particular emphasis has been placed on establishing absorption features related to the presence of EPR resonances at g 5, 1.78 and 1.69, which have been tentatively assigned to a spin-coupled state involving cytochrome a₃ and ‘EPR-undetectable Cu’ (Beinert, H., Shaw, R.W., Dunham, R.W. and Sands, R.H. (1982) in Oxidases and Related Redox Systems (King, T.E., Mason, H.S. and Morrison, M., eds.), Pergamon Press, Oxford, in the press). For optical studies we have used a versatile rapid-scanning spectrophotometer to obtain well resolved spectra down to 2 ms reaction time. Concomitant with the appearance (within 10 ms) of EPR signals at g 5, 1.78 and 1.69 is the presence of an enhanced absorption (Δε = 0.25 mM (heme a)^?1·cm^?1) at 660 nm, with a trough (relative to following spectra) at 580 nm. In our hands, this feature disappears in a first-order process with a half-life of 46 s at pH 7.2 and 2°C. The effect of this spectral transformation is to decrease considerably the acuteness of the 655 nm absorption band, previously suggested as representing a state of the enzyme in which ferric cytochrome a₃ is coupled to oxidised EPR-undetectable Cu (Beinert, H., Hansen, R.E. and Hartzell, C.R. (1976) Biochim. Biophys. Acta 423, 339–355). This observation can be correlated satisfactorily with a small field shift of the high-field resonances at g 1.78 and 1.69 and a broadening at g 1.78. Support for this and further correlative assignments arises from parallel experiments using cytochrome c oxidase purified via an alternative procedure, which displays different kinetic behavior. Further transformations of the oxidized enzyme are evident through an approx. 10% decrease in absorbance at 600 nm together with small changes centered at 640 and 665 nm (which serve to restore the sharpness of the 655 nm band). The kinetics, as analyzed by the Guggenheim procedure using the absorbance at 597 nm, indicate approx. 50% first-order linearity (half-life 40 min) with additional species contributing at longer times, while over a parallel time course (0–3 h) the EPR resonances at g 5, 1.78 and 1.69 virtually disappear. These novel signals can also be seen at a lower intensity in samples of cytochrome c oxidase anaerobically reoxidized by porphyrexide and frozen after a 6 min incubation period at 4°C. This observation, along with the establishment of similar optical changes over the time course of 1 min to 3 h, suggests that aerobic and anaerobic reoxidation produce common forms of the enzyme. Comparison of the g 1.78 and 1.69 resonances between samples rapidly aerobically reoxidized in the presence of H₂¹⁶O and H₂¹⁷O yielded no evidence for the presence of any labile oxygen ligand (including OH^?, H₂O) in the coordination sphere of the species involved.     

Zur gegenwärtigen problematik der evolutionsforschung

Reflections on the actual problematics of the palaeontological evolution research are observed under epistemological aspects. When discussing new or only pretended new beginnings, sometimes with claim to neutral-point elucidations, success and merit of the traditional methods in palaeontology should not be forgotten. Gradualism and punctualism reduce the multilateral reality of nature.     

Amino acid sequence of the active site of human pseudocholinesterase

The usualE ₁ ^u and atypicalE ₁ ^a human pseudocholinesterases (acylocholine acylhydrolase, EC 3.1.1.8) were purified to homogeneity. The active-site serine residue was conjugated with diisopropyl fluorophosphate and digested with trypsin. The tryptic peptide containing the active site was isolated by gel filtration followed by two-dimensional paper chromatography and electrophoresis. The amino acid sequence of the active site peptide obtained from the usualE ₁ ^u enzyme was found to be Gly-Glu-Ser-Ala-Gly-Ala-Ser-Ala-Val-Ser-Leu. A remarkable structural homology exists between the human and the horse enzymes in their active sites. From the difference in electrophoretic mobility of the active-site peptides obtained from the usual and atypical enzymes, the probable structure of the atypical human enzyme was deduced as Gly-His-Ser-Ala-Gly-Ala-Ser-Ala-Val-Ser-Leu.