561 resultados para 1160
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Sign.: []8, a-c8, d4, e-i8, k10, 2a-2d8, 2e6, 2f-2g8, 2h6, A-F8, G4, H-I8, K4, 4a8, 4b10, 4c8, 4d10, 4e4, 2[alfa]-2[delta]8, 2[épsilon]4
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Sign.: []8, a-c8, d4, e-i8, k10, 2a-2d8, 2e6, 2f-2g8, 2h6, A-F8, G4, H-I8, K4, 4a8, 4b10, 4c8, 4d10, 4e4, 2[alfa]-2[delta]8, 2[épsilon]4
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Lugar e imp. tomados del colofón en E6r
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Marca tip. en port. (Sivestre. Marques, 708)
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Copia digital: Biblioteca Valenciana, 2011
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Marca tip. en port
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Informativo consulex: paginação decrescente.
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Megalin (gp330), an epithelial endocytic receptor, is a major target antigen of Heymann nephritis (HN), an autoimmune disease in rats. To elucidate the mechanisms of HN, we have mapped a pathogenic epitope in megalin that binds anti-megalin antibodies. We focused our attention on four clusters of cysteine-rich, low density lipoprotein receptor (LDLR) ligand binding repeats in the extracellular domain of megalin because they represent putative ligand binding regions and therefore would be expected to be exposed in vivo and to be able to bind circulating antibodies. Rat megalin cDNA fragments I through IV encoding the first through fourth clusters of ligand-binding repeats, respectively, were expressed in a baculovirus system. All four expression products were detected by immunoblotting with two antisera capable of inducing passive HN (pHN). When antibodies eluted from glomeruli of rats with pHN were used for immunoblotting, only the expression product encoded by fragment II was detected. This indicates that the second cluster of LDLR ligand binding repeats is directly involved in binding anti-megalin antibodies and in the induction of pHN. To narrow the major epitope in this domain, fragment II was used to prepare proteins sequentially truncated from the C- and N-terminal ends by in vitro translation. Analysis of the truncated translation products by immunoprecipitation with anti-megalin IgG revealed that the fifth ligand-binding repeat (amino acids 1160-1205) contains the major epitope recognized. This suggests that a 46-amino acid sequence in the second cluster of LDLR ligand binding repeats contains a major pathogenic epitope that plays a key role in pHN. Identification of this epitope will facilitate studies on the pathogenesis of HN.
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Title from f. 1v.
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lil-ʻalāmah Abī al-Ḥasan ʻAlī ibn Abī al-Karam Muḥammad ibn Muḥammad ibn ʻAbd al-Karīm ibn ʻAbd al-Wāḥid al-Shaybānī al-maʻrūf bi-Ibn al-Athīr al-Jazarī al-mulaqqab bi-ʻIzz al-Dīn. Wa-bi-hāmishihi Tārīkh murūj al-dhahab wa-maʻādin al-jawhar / lil-Imām Abī al-Ḥasan ʻAlī ibn al-Ḥusayn al-Masʻūdī.
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Copy completed in Rabīʻ al-Ākhir 1160 [1747].
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Dated 1106 [1694-5] but it appears to be a mistake, the correct date should be 1160 [1747].
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Copy completed in 1160 [1747] in the hand of Muḥammad ibn Ḥusayn.
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In Cruise 13 of R/V Akademik Sergey Vavilov in the Pechora Sea, six heat flow varied from 50 to 75 mW/m**2. Deep heat flow in the Pechora Sea was calculated equal to 45 mW/m**2, which is confirmed by results of geological and geophysical studies and corresponds to Middle Baikal age of the basement. A model of structure of the lithosphere in the Pechora Sea is suggested. Total thickness of the lithosphere in the basin (190 km) determined from geothermal data agrees well with that in transition zones from the continent to the ocean. According to estimates of deep heat flow in the region obtained, thickness of the mantle (160 km), of the basaltic (15 km), and of the granitic (15 km) layers of the lithosphere were also evaluated. Temperature values at boundaries of the sedimentary layers were calculated over a geological and geophysical profile crossing the Pechora Sea basin. Temperatures obtained agree with the temperature interval of hydrocarbon generation and correspond to Permian-Triassic sedimentary sequences, which are the most productive ones in the Pechora Sea region from the point of view of oil and gas potential.