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Digitalisat der Ausg. Presburg, [1863/64]

Inerlekh parṭeyishe fragn fun Al.K.P.(B.)

Y. Sṭalin

B, d11B, K and d18O data for altered oceanic crust at DSDP Sites 417/418

Samples of drilled oceanic crust, from DSDP Holes 417A, 417D and 418A and ODP Hole 735B, and oceanic crust from the Oman and Cyprus ophiolites, were analyzed for B contents and d11B. Composite samples from DSDP Holes 417A, 417D and 418A were used to represent the upper 550 m of altered oceanic crustal Layer 2A. Whole-rock samples from the Troodos ophiolite, Cyprus, and the Oman ophiolite were selected to represent crustal Layer 2B dikes. Composite samples from ODP Hole 735B were used to represent crustal Layer 3. The B content of the DSDP composites ranges from 7.2 ppm to 104 ppm and correlates with both d1818O and K, showing that it is a good indicator of the extent of low temperature alteration. The d11B of the DSDP composites varies between -2.5? and 5.4?. The B content of the samples from the Troodos ophiolite ranges from 2.4 ppm to 8.1 ppm; d11B varies from -0.9? to 7.8?. The B content of the Oman ophiolite samples ranges from 5.0 ppm to 11.1 ppm; d11B varies from -1.6? to 16.9?. The B content of the samples from ODP Hole 735B ranges from 1.1 ppm to 7.1 ppm; d11B varies from -4.3? to 24.9?. The general pattern displayed by these samples is one of greatest (and most variable) B enrichment at the top of the crust and least enrichment at the bottom of the section. All of these samples are enriched compared to unaltered MORB, which is believed to have a B content of approximately 0.5 ppm. The d11B values of deeper samples, from Layers 2B and 3, are more variable and generally higher than those from Layer 2A. Boron contents and d11B are not correlated. The data from the DSDP Site 417/418 composites indicate that the d11B of fluid circulating in the upper crust changes only slightly during alteration, increasing by an average of 5.1? with an accompanying decrease in B concentration of 7%. Low temperature alteration appears to be a water-dominated process resulting in minor modification of circulating seawater. A minimum water-rock ratio of 400 is calculated for these samples, implying a minimum low-temperature seawater flux through the upper oceanic crust of 3.4?10**14 l/y. The average B content of altered oceanic crust, as represented by these samples, is 5.2+/-1.7 ppm and the average d11B is 3.4+/-1.1?. This average isotopic composition is measurably different from the apparent average of oceanic sediments, supporting the idea that d11B could be useful for identifying the source(s) of B in island arcs.

Purification and characterization of a CENP-B homologue protein that binds to the centromeric K-type repeat DNA of Schizosaccharomyces pombe

We have purified and characterized a novel 60-kDa protein that binds to centromeric K-type repeat DNA from Schizosaccharomyces pombe. This protein was initially purified by its ability to bind to the autonomously replicating sequence 3002 DNA. Cloning of the gene encoding this protein revealed that it possesses significant homology to the mammalian centromere DNA-binding protein CENP-B and S. pombe Abp1, and this gene was designated as cbh+ (CENP-B homologue). Cbh protein specifically interacts in vitro with the K-type repeat DNA, which is essential for centromere function. The Cbh-binding consensus sequence was determined by DNase I footprinting assays as PyPuATATPyPuTA, featuring an inverted repeat of the first four nucleotides. Based on its binding activity to centromeric DNA and homology to centromere proteins, we suggest that this protein may be a functional homologue of the mammalian CENP-B in S. pombe.

Defective γ-aminobutyric acid type B receptor-activated inwardly rectifying K+ currents in cerebellar granule cells isolated from weaver and Girk2 null mutant mice

Stimulation of inhibitory neurotransmitter receptors, such as γ-aminobutyric acid type B (GABAB) receptors, activates G protein-gated inwardly rectifying K+ channels (GIRK) which, in turn, influence membrane excitability. Seizure activity has been reported in a Girk2 null mutant mouse lacking GIRK2 channels but showing normal cerebellar development as well as in the weaver mouse, which has mutated GIRK2 channels and shows abnormal development. To understand how the function of GIRK2 channels differs in these two mutant mice, we compared the G protein-activated inwardly rectifying K+ currents in cerebellar granule cells isolated from Girk2 null mutant and weaver mutant mice with those from wild-type mice. Activation of GABAB receptors in wild-type granule cells induced an inwardly rectifying K+ current, which was sensitive to pertussis toxin and inhibited by external Ba2+ ions. The amplitude of the GABAB receptor-activated current was severely attenuated in granule cells isolated from both weaver and Girk2 null mutant mice. By contrast, the G protein-gated inwardly rectifying current and possibly the agonist-independent basal current appeared to be less selective for K+ ions in weaver but not Girk2 null mutant granule cells. Our results support the hypothesis that a nonselective current leads to the weaver phenotype. The loss of GABAB receptor-activated GIRK current appears coincident with the absence of GIRK2 channel protein and the reduction of GIRK1 channel protein in the Girk2 null mutant mouse, suggesting that GABAB receptors couple to heteromultimers composed of GIRK1 and GIRK2 channel subunits.

Human γ-aminobutyric acid type B receptors are differentially expressed and regulate inwardly rectifying K+ channels

γ-Aminobutyric acid type B receptors (GABABRs) are involved in the fine tuning of inhibitory synaptic transmission. Presynaptic GABABRs inhibit neurotransmitter release by down-regulating high-voltage activated Ca2+ channels, whereas postsynaptic GABABRs decrease neuronal excitability by activating a prominent inwardly rectifying K+ (Kir) conductance that underlies the late inhibitory postsynaptic potentials. Here we report the cloning and functional characterization of two human GABABRs, hGABABR1a (hR1a) and hGABABR1b (hR1b). These receptors closely match the pharmacological properties and molecular weights of the most abundant native GABABRs. We show that in transfected mammalian cells hR1a and hR1b can modulate heteromeric Kir3.1/3.2 and Kir3.1/3.4 channels. Heterologous expression therefore supports the notion that Kir3 channels are the postsynaptic effectors of GABABRs. Our data further demonstrate that in principle either of the cloned receptors could mediate inhibitory postsynaptic potentials. We find that in the cerebellum hR1a and hR1b transcripts are largely confined to granule and Purkinje cells, respectively. This finding supports a selective association of hR1b, and not hR1a, with postsynaptic Kir3 channels. The mapping of the GABABR1 gene to human chromosome 6p21.3, in the vicinity of a susceptibility locus (EJM1) for idiopathic generalized epilepsies, identifies a candidate gene for inherited forms of epilepsy.

Kitāb-i Ādāb al-mulūk

[Muḥammad Rafīʻ ibn ʻAlī Aṣghar al-Ṭab��ṭab��ʼī].