Beiträge zur Kenntnis der Zusammensetzung Fetter Öle in verschiedenen Teilen einer Pflanze

Ohne ZusammenfassungMit 1 Textabbildung.Dissertation der Philosophischen Fakultät der Universität Leipzig.     

Sarcomere length uniformity determined from three-dimensional reconstructions of resting isolated heart cell striation patterns.

A- and I-band striation positions have been obtained, three-dimensionally reconstructed, and statistically analyzed from the volumes of resting isolated heart cells. Striation patterns from optically discrete subvolumes are imaged along the length of these myocytes with a computer-interfaced optical microscope imaging system. Planar striation maps are reconstructed by the computer from sequentially obtained striation pattern images displaced across the width or depth of the cell in controlled steps. Multiple planar maps are combined to form full three-dimensional (3-D) reconstructions that illustrate the sarcomeric structure and ordering throughout the volume of the cell. These reconstructions demonstrate a high degree of striation registration throughout most regions of cardiac cells. The striation registration is often slightly (less than 10 degrees) skewed across the width or depth of nearly every cell and is occasionally disrupted between adjacent groups of sarcomeres. These disruptions in registration are always associated with the locations of the nuclei. Rigorous statistical analyses indicate small volumetric regions of the cell delineated by these disruptions can have significantly (0.014-0.113 micron) shorter or longer average sarcomere length periodicities. Unlike skeletal muscle "fibrillenstruktur," these data from cardiac cells exhibit no evidence of helical packing schemes for sarcomere order. These observations suggest that the relatively large nuclei displace and disrupt the normal registration of the sarcomeres, which is probably mediated by internal cytoskeletal structures.     

Fluorescence characteristics of cyanobacteria (blue-green algae)

The fluorescence characteristics of the cyanobacteria Synechocystisaquatilis Sauv., Microcystis firma (Breb. et Lenorm.) Schmidleand Synechococcus leopoliensis (Racib.) Kom. and the green algaScenedesmus quadricauda (Turp.) Breb. were examined. In thethree cyanobacteria, phycocyanin is the main accessory pigment.Phycoerythrin is not present in our investigated strains ofcyanobacteria. The highest excitation of the chlorophyll a (Chla) fluorescence of cyanobacteria resulted from light with wavelengthsof 620–630 nm. A definite ‘Kautsky’ effectis also evident at this wavelength. However, excitation withblue light (420–520 nm) produced only very slight fluorescence.The Kautsky effect is not evident at these wavelengths, evenat high photon flux densities. For Scenedesmus, fluorescencecharacteristics typical of green algae were found. The fluorescenceexcitation of cyanobacteria at 620 nm corresponds to a photosynthesispeak in the action spectrum measured in terms of O₂ production.The results underline the necessity of fluorescence measurementsat several wavelengths whenever mixed populations are involved.Such measurements also present possibilities for more accurateestimation of biomass and potential photosynthetic productionin mixed populations.     

Absence of Turner stigmata in a 46,XYp-female

A 46,XY female patient with streak gonads and a large deletion of Yp is described. The deletion included the Y chromosomal genes SRY, ZFY, and RPS4Y. The patient did not display any Turner stigmata, such as webbing of the neck, cardiac or other abnormalities. The findings argue against an important role of RPS4Y in the prevention of Turner stigmata in males and are consistent with a role of SRY in testis differentiation in humans.     

Monoclonal antibodies to bovine UDP-galactosyltransferase. Characterization, cross-reactivity, and utilization as structural probes

A series of mouse monoclonal antibodies has been developed against a soluble form of bovine UDP-galactose:N-acetylglucosamine galactosyltransferase purified to apparent chemical homogeneity by a combination of affinity and immunoadsorption chromatography. The purified enzyme consists of two molecular mass variants of 42 and 48 kDa. Individual monoclonal antibodies were selected for by their ability to recognize immobilized affinity-purified galactosyltransferase and were not reactive against bovine alpha-lactalbumin and bovine immunoglobulins. Based on competitive binding assays and Western blot analysis with either galactosyltransferase or lactose synthetase (covalently cross-linked alpha-lactalbumin galactosyltransferase), these monoclonal antibodies can be subdivided into four groups. Group A (3 clones) recognize an epitope at or near the alpha-lactalbumin binding site. In addition, this group is cross-reactive with soluble galactosyltransferase from human milk and pleural effusion. Group B (6 clones) and D (1 clone) appear to recognize two different epitopes on the 6-kDa fragment which is released when the 48-kDa galactosyltransferase polypeptide is converted to the 42-kDa form, apparently by proteolysis. Groups A and C (1 clone) recognize epitopes found on both the 48- and 42-kDa polypeptide. Interestingly, immunofluorescence studies indicate that only two monoclonal antibody groups (C and D) are able to decorate membrane-bound galactosyltransferase (Golgi-associated) in formalin-fixed, methanol-, or detergent-permeabilized cells. Thus, these groups of monoclonal antibodies appear to identify four separate structural/functional domains on soluble galactosyltransferase, two of which are not readily accessible for binding in situ.     

Effects of stormwater sewer discharges on the aquatic community in urban canals in Lelystad

In urban areas with a separate sewerage system, the stormwater runoff is discharged into surface waters. A study on the effects of stormwater sewer discharges on the composition of the aquatic community in urban waters was carried out in two areas with a primarily residential use in the new town of Lelystad. The aquatic organisms considered included hydrophytes, epiphytic diatoms, filamentous algae and macroinvertebrates.The results indicate that the stormwater sewer discharges cause a slight change in the composition of the aquatic community. The water in the urban surface waters can be characterized as eutrophic and - toa-mesosaprobic. Near stormwater sewer outfalls the water tends to the more polluteda-mesosaprobic state. The shifts in the composition of the aquatic community could be traced primarily on the basis of a number of epiphytic diatoms and macroinvertebrates (in particular some Diptera and Trichoptera). Most hydrophytes, filamentous algae and the remaining epiphytic diatoms and macroinvertebrates (in particular water beetles and water mites) turned out to be of little or no use in this respect.Because the investigation was carried out in an unusually dry summer, the results probably underestimate the effects of stormwater discharges on the aquatic community.     

Der Turnover der Proteine in den Organen des Flußkrebses Orconectes limosus

Zusammenfassung Aus dem exponentiellen Abfall der spezifischen Aktivität nach einmaliger Injektion von L-Leucin-¹⁴C wurden die Halbwertszeiten der Gesamtproteine in den meisten Organen des Mußkrebses zu 8,5–19 Tagen bestimmt, in Leber und Niere der Maus zu 1,6–1,7 Tagen. Muskel- und Hämolymphproteine des Krebses zeigten weit längere Halbwertszeiten. Berücksichtigt man die Temperaturdifferenz von 25° unter Annahme eines Q ₁₀ von 2,0–2,5, so ergeben sich für Maus und Krebs etwa übereinstimmende Geschwindigkeiten des Proteinturnovers.

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Protein turnover in the tissues of the crayfish, Orconectes limosus

Summary The exponential decay of protein radioactivity after injection of L-Leucin-¹⁴C was measured in the different tissues of the crayfish, and in liver and kidney of the mouse. The half life time of tissue proteins was calculated to be 8.5 to 19 days in most crayfish tissues, 1.6 to 1.7 days in the mouse liver and kidney. Proteins of muscle and hemolymph of crayfish had much longer half life values. Taking into consideration the temperature difference of 25° C and assuming a Q ₁₀ of 2.0 to 2.5, the speed of protein turnover corresponds in the mouse and the crayfish.

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