The chemical-transformation products of 1,6-dibromo-1,6-dideoxygalactitol and 1,2:5,6-dianhydrogalactitol in aqueous solution

After hydrolysis of 1,6-dibromo-1,6-dideoxygalactitol (1) and 1,2:5,6-dianhydrogalactitol (2), 11 compounds were isolated, three of them as tritylated derivatives. Their structures were established on the basis of chemical evidence and, for four compounds, by X-ray diffraction. The main product of the hydrolysis of 1 was 3,6-anhydro-1-bromo-1-deoxy-dl-galactitol; the end-products of the hydrolysis of 2 were 1,5-anhydro-dl-galactitol, 2,5-anhydro-dl-altritol, and galactitol.     

Über die Verteilung epiphytischer Algen auf den Blättern wasserbewohnender Angiospermen sowie systematisch-entwicklungsgeschichtliche Bemerkungen über einige grüne Algen

Ohne Zusammenfassung     

Transplantation of insect giant chromosome nuclei into amphibian oocytes

Polytene salivary gland nuclei of Chironomus pallidivittatus were transplanted into oocytes of Xenopus laevis which were then cultured in vitro for 18 h. The giant chromosomes and nucleoli as well as the entire nuclei enlarged considerably in volume during this time. The polyteny and specific chromomere pattern of the chromosomes were maintained, and the puffing of the salivary gland-specific Balbiani rings was not noticeably changed. — Polytene nuclei from differentiated insect cells transplanted into Xenopus oocytes thus appear suited for exposing giant chromosomes in vivo to purified factors such as regulatory molecules. This paper is dedicated to Professor Wolfgang Beermann on the occasion of his 60th birthday     

Cloning, structure and expression of a cDNA encoding the human androgen receptor

A cDNA clone has been isolated from a library prepared of mRNA of human breast cancer T47D cells with an oligonucleotide probe homologous to part of the region encoding the DNA-binding domain of steroid receptors. The clone has a size of 1505 bp and sequence analysis revealed an open reading frame of 1356 bp. The deduced amino acid sequence displays two highly conserved regions identified as the putative DNA-binding and hormone binding domains respectively of steroid receptors. Expression of this cDNA clone in COS cells produces a nuclear protein with all the binding characteristics of the human androgen receptor (hAR). The gene encoding the cDNA is assigned to the human X-chromosome. High levels of three hybridizing mRNA species of 11, 8.5 and 4.7 kb respectively are found in the human prostate cancer cell line (LNCaP), which contains elevated levels of hAR. The present data provide evidence that we have isolated a cDNA that encodes a major part of the human androgen receptor.     

Effects of octopamine on miniature excitatory junction potentials from developing and adult moth muscle

Intracellular recordings of excitatory junction potentials (EJPs) and miniature EJPs (MEJPs) were made from the dorsal longitudinal muscle of Manduca sexta to determine the sites of action of octopamine. MEJPs increased in amplitude and frequency as the moth developed during the 3 days before eclosion. DL-Octopamine (5 X 10(-6) M) increased the amplitude of excitatory junction potentials in both immature moths (one day before eclosion) and adults. Octopamine (10(-5) M) also increased the amplitude and frequency of MEJPs from immature animals (one and two days before eclosion) but had the opposite effect on adults and pharate adults ready to eclose. Treatment with octopamine (10(-5) M) resulted in a decrease in input resistance and a hyperpolarization in both immature and adult muscle fibers. The results suggest that octopamine acts both presynaptically and postsynaptically but that the increase in the amplitude of the evoked response is due primarily to influences on presynaptic processes.     

Phosphate-Activated Glutaminase in the Crude Mitochondrial Fraction (P2 Fraction) from Human Brain Cortex

The kinetics and other properties of phosphate-activated glutaminase have for the first time been studied in the crude mitochondrial fraction (P2 fraction) from human brain. The enzyme is for unexplained reasons inactivated postmortem. The enzyme activity decreases by storing the tissue or homogenate at 37 degrees C. The inactivation is not caused by formation of a dialysable inhibiting compound. No large proteolytic degradation has occurred, since the phosphate-activated glutaminase-like immunoreactive band did not disappear during the storage. The molecular weight of the subunit of the enzyme as determined by immunoblots of sodium dodecyl sulfate-treated homogenates from human brain is estimated to be approximately 64 K. The enzyme has been shown to have a pH optimum of 8.6; it is activated by phosphate, inhibited by glutamate, and partially inhibited by ammonia. Double-inverse plots of enzyme activity against phosphate are concave-upward, and more so in the presence of an inhibitor. The inhibition by glutamate appears to be noncompetitive with the substrate glutamine, and competitive with the activator phosphate. These kinetic properties are not significantly different from our earlier observations concerning phosphate-activated glutaminase from pig brain and pig kidney.     

The Fc-receptor III of cultured human monocytes. Structural similarity with FcRIII of natural killer cells and role in the extracellular lysis of sensitized erythrocytes

FcRIII is not present on peripheral blood monocytes, but becomes expressed upon culturing and can be demonstrated on tissue macrophages. We studied the expression of FcRIII of cultured monocytes in detail and compared its structure with FcRIII of neutrophils and NK cells. The cell density of FcRIII reached a plateau within 3 days of culturing. During that time, the expression of FcRI and FcRIIa, also present on monocytes, did not change significantly. FcRIII on cultured monocytes lacked, as did NK cell FcRIII, the NA1-allotypic variant of the NA system present on the neutrophil FcRIII. Studies with glycosyl-phosphatidyl-inositol-specific phospholipase C and analysis of cells of patients with paroxysmal nocturnal hemoglobinuria revealed that FcRIII on cultured monocytes is not anchored by phosphatidyl-inositol-glycan in the cell membrane. Similarly, FcRIII on NK cells was resistant to glycosyl-phosphatidyl-inositol-specific phospholipase C treatment, suggesting that NK cell FcRIII is also not anchored by a phosphatidyl-inositol-glycan moiety, in contrast to neutrophil FcRIII. Analysis by SDS-PAGE showed that the FcRIII of cultured monocytes had a similar mobility as the FcRIII on NK cells, but was clearly distinct from neutrophil FcRIII. Treatment with N-glycanase showed that the protein backbone of deglycosylated FcRIII of cultured monocytes was similar to that of FcRIII of NK cells, but deglycosylated neutrophil FcRIII was different. Specific blocking of FcRIII of cultured monocytes with an anti-FcRIII mAb did not reduced the lytic action of the cultured monocytes towards sensitized erythrocytes. However, FcRIII was modulated from the cell surface by incubation with sensitized E, whereas non-FcR Ag were not. These findings indicate that FcRIII is involved in binding of immune complexes, but does not act as a trigger molecule for extracellular lysis of sensitized E.