Satelliten-Telemetrie bei einem juvenilen Schreiadler (Aquila pomarina) auf dem Herbstzug

Zusammenfassung 1992 konnte ein Schreiadler mit Hilfe der Satelliten-Telemetrie nach dem Abzug aus dem Brutgebiet in Mecklenburg-Vorpommern 2125 km weit verfolgt werden. Die Ortung erfolgte durch das AGROS-System. Der Abzug erfolgte am 16. oder 17. August in SE-Richtung. Nach 660 km Luftlinie in den polnisch-slowakischen West-Beskiden schwenkte der Vogel nach Süden ab und flog fast geradlinig zwischen dem 19 ° und 22 ° E weite auf dem kürzesten Weg in Richtung Nordafrika, bis er nach 1340 km am 29. September im äußersten Südwesten des Peloponnes eintraf. Dort zögerte er, seinen Zug fortzusetzen und flog mindestens 12 Tage in nördlicher und südlicher Richtung an der Westküste hin und her. Das plötzliche Ausbleiben von Signalen nach dem 8. Oktober bei bestem Ladezustand der Batterien wird dahingehend gedeutet, daß der Adler abgeschossen wurde oder bei dem Versuch, das Mittelmeer zu überqueren, umkam.

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Satellite tracking of a juvenile Lesser Spotted Eagle (Aquila pomarina) during autumn migration

Summary In 1992, for the first time a Lesser Spotted Eagle was tracked with a satellite transmitter (PTT) for 2,125 km on its migration route from its birthplace in Mecklenburg-Vorpommern (Northern Germany). Locations were obtained by the ARGOS system. The migration began on 16 or 17 August in a south-easterly direction. After 660 km the young eagle veered south in the Beskidy mountains on the Polish-Slovak border (about 80 km south of Katowice) and flew in an almost straight line between 19 ° and 22 ° E on the shortest route to North Africa (not towards the Bosphorus) until after covering another 1,340 km it reached the extreme south-west of the Peloponnese (Greece) on 24 September. There it lingered for at least 12 days flying north and south, up and down the west coast before probably continuing on its migration. The abrupt cessation of signals after 8 October, notwithstanding the prime condition of the batteries, indicated that the eagle had been shot or perished in an attempt to cross the Mediterranean.

     

Biotransformation of diphenyl ether by the yeastTrichosporon beigelii SBUG 752

Trichosporon beigelii SBUG 752 was able to transform diphenyl ether. By TLC, HPLC, GC, GC-MS, NMR- and UV-spectroscopy, several oxidation products were identified. The primary attack was initiated by a monooxygenation step, resulting in the formation of 4-hydroxydiphenyl ether, 2-hydroxydiphenyl ether and 3-hydroxydiphenyl ether (48:47:5). Further oxidation led to 3,4-dihydroxydiphenyl ether. As a characteristic product resulting from the cleavage of an aromatic ring, the lactone of 2-hydroxy-4-phenoxymuconic acid was identified. The possible mechanism of ring cleavage to yield this metabolite is discussed.     

Calliphorin,a major protein of the blowfly: Correlation between the amount of protein,its biosynthesis,and the titer of translatable calliphorin-mRNA during development

The amount of calliphorin, its biosynthesis, and the levels of translatable calliphorin-mRNA have been determined during the postembryonic development of Calliphora vicina R.-D. The amount of calliphorin increases in early third-instar larvae, reaching maximal levels in 6-day-old animals. It continuously decreases during late larval and pupal development to approximately one-half of the maximal levels and abruptly sinks during eclosion. The biosynthesis of calliphorin takes place only in 3- to 5-day-old larvae. Poly(A)⁺-RNA has been translated into proteins in a wheat germ cell-free system. Calliphorin-mRNA can be detected in 3- to 7-day-old larvae; maximal concentrations are observed in 4- and 5-day-old animals. No calliphorin-mRNA can be detected in prepupae, pupae, or imagos. The biosynthesis of calliphorin in blowfly larvae stops before a decrease of translatable calliphorin-mRNA is observed. This finding raises the question of the mechanism of in vivo inactivation of this specific mRNA.     

Complete cDNA and gene sequence of the developmentally regulated arylphorin of Calliphora vicina and its homology to insect hemolymph proteins and arthropod hemocyanins.

Two cDNA libraries were prepared from poly(A)+ RNA isolated from fat bodies of last instar larvae of the blowfly Calliphora vicina. The libraries were probed with a genomic clone containing the coding sequence for an arylphorin subunit. Two cDNA clones as well as the genomic clone were mapped and their nucleotide sequences were determined. This revealed the presence of an open reading frame corresponding to a polypeptide with 759 amino acid residues. The deduced primary structure of Calliphora arylphorin and hemolymph proteins of other insect species and arthropod hemocyanine show nearly 30% identity. Highly conserved regions could be also identified.     

Multiple components of a complex androgen-dependent enhancer.

Sex-limited protein (Slp) is expressed in adult male mice. A 160-basepair fragment 2 kilobases upstream of the gene serves as an androgen-dependent enhancer of chloramphenicol acetyltransferase expression in transient transfection assays in cells with endogenous or cotransfected androgen receptor. One element that is necessary, but not sufficient, for induction is a consensus glucocorticoid (or hormone) response element (HRE). This element binds to the mouse androgen receptor in vitro, but with apparent weak affinity. Induction by the HRE is greatly augmented by an accessory sequence within the 160 basepairs, suggesting that cooperative interactions confer strong response to androgen. Additional elements within the enhancer modulate induction, positively or negatively, and exhibit cell-specific behavior. Of particular interest are two degenerate HREs that are adjacent to the consensus sequence; they show no independent activity, but are functionally significant in conjunction with other elements. The complexity of this enhancer may reflect biological mechanisms that ensure specificity of hormonal response and allow gene expression to respond to changes in hormone concentration.     

Differential expression of the p65 gene family

The genome of the marine ray Discopyge ommata contains at least three p65-related genes. o-p65-A is 84% identical, o-p65-B is 78% identical, and o-p65-C is only 41% identical to a previously characterized rat p65. The cytoplasmic domain, particularly the two regions that are similar to the regulatory domain of protein kinase C, are most highly conserved. The three genes are expressed in different but overlapping patterns in the central nervous system. o-p65-A immunoreactivity is found predominantly in forebrain, cerebellum, and neuroendocrine cells, while o-p65-B immunoreactivity is predominantly localized to the spinal cord, brainstem, and midbrain. Many synaptic vesicle proteins are members of small gene families that are differentially expressed, resulting in several unique combinations of these molecules in specific brain regions.     

Discrete regions of simian virus 40 large T antigen are required for nonspecific and viral origin-specific DNA binding.

The nondefective adenovirus type 2 (Ad2)-simian virus 40 (SV40) hybrid viruses, Ad2+ND2 and Ad2+ND4, have been used to determine which regions of the SV40 genome coding for the large tumor (T) antigen are involved in specific and nonspecific DNA binding. Ad2+ND2 encodes 45,000 M4 (45K) and 56,000 Mr (56K) T antigen-related polypeptides. The 45K polypeptide did not bind to DNA, but the 56K polypeptide bound nonspecifically to calf thymus DNA, Ad2+ND4 encodes 50,000 Mr (60K), 66,000 Mr (66K), 70,000 Mr (70K), 74,000 Mr (74K), and 90,000 Mr (90K) T antigen-related polypeptides, all of which bound nonspecifically to calf thymus DNA. However, in more stringent assays, where tight binding to viral origin sequences was tested, only the 90K protein specified by Ad2A+ND4 showed specific high affinity for sequences at the viral origin of replication. From these results and previously published experiments describing the SV40 DNA integrated into these hybrid viruses, it was concluded that SV40 early gene sequences located between 0.39 and 0.44 SV40 map units contribute to nonspecific DNA binding, whereas sequences located between 0.50 and 0.63 SV40 map units are necessary for specific binding to the viral origin of replication.