Multispectral Imaging Data of Ms. or. quart. 1105 and Ms. or. quart. 1121 of Staatsbibliothek zu Berlin

Multispectral Imaging Data of selected areas of erased writing of Ms. or. quart. 1105 and Ms. or. quart. 1121 captured on the 31 of May 2017 at the Centre for the Study of Manuscript Cultures (CSMC) while both manuscripts were being catalogued. The manuscripts are owned by Staatsbibliothek zu Berlin. Ms. or. quart. 1105 is an Arabic multiple-text manuscript of thirteen treatises on various Christian subjects written on parchment. Some of them are translations from Greek texts. Ms. or. quart. 1121 is an Arabic composite manuscript of two texts written on paper. The first work consists of the tenth part of a biographical work, which was made a bequest to a library in Kairo in 761 hijra /1359-60 AD by a former owner. The last text, being a mystical treatise, was copied in 1050 hijra / 1641 AD

Die Refaiya aus Damaskus: Eine alte arabische Bibliothek geht in Leipzig online

In Deutschland boomt die Digitalisierung der Bibliotheken und Archive. Der Trend geht eindeutig in Richtung virtuelle Bibliothek mit über das Internet abrufbaren Beständen. Auch die kleinen „Orchideenfächer“ sind aktiv geworden. Erste Projekte zur Digitalisierung von orientalischen Handschriften, Papyri und Ostraka wurden bereits erfolgreich abgeschlossen

p53 Protein Exhibits 3′-to-5′ Exonuclease Activity

AbstractHighly purified p53 protein from different sources was able to degrade DNA with a 3′-to-5′ polarity, yielding deoxynucleoside monophosphates as reaction products. This exonuclease activity was dependent on Mg2+ and inhibited by addition of 5 mM nucleoside monophosphates. This exonuclease activity is intrinsic to the wild-type p53 protein: it copurified with p53 during p53 preparation; only purified wild-type p53, but not identically purified mutant p53 proteins displayed exonuclease activity; the exonuclease activity could be reconstituted from SDS gel-purified and urea-renatured p53 protein and mapped to the core domain of the p53 molecule; and finally, purified p53 protein could be UV cross-linked to GMP. A p53-intrinsic exonuclease activity should substantially extend our view on the role of p53 as a “guardian of the genome.

NSP4 Is Stored in Azurophil Granules and Released by Activated Neutrophils as Active Endoprotease with Restricted Specificity

Whereas neutrophil elastase, cathepsin G, and proteinase 3 have been known as granule-associated serine proteases of neutrophils for decades, a fourth member, called neutrophil serine protease 4 (NSP4), was just recently described and provisionally characterized. In this study, we identified NSP4 as a novel azurophil granule protein of neutrophils by Western blot analyses of subcellular fractions as well as by RT-PCR analyses of neutrophil precursors from human bone marrow. The highest mRNA levels were observed in myeloblasts and promyelocytes, similar to myeloperoxidase, a marker of azurophil granules. To determine the extended sequence specificity of recombinant NSP4, we used an iterative fluorescence resonance energy transfer-based optimization strategy. In total, 142 different peptide substrates with arginine in P1 and variations at the P1', P2', P3, P4, and P2 positions were tested. This enabled us to construct an alpha(1)-proteinase inhibitor variant (Ile-Lys-Pro-Arg-/-Ser-Ile-Pro) with high specificity for NSP4. This tailor-made serpin was shown to form covalent complexes with all NSP4 of neutrophil lysates and supernatants of activated neutrophils, indicating that NSP4 is fully processed and stored as an already activated enzyme in azurophil granules. Moreover, cathepsin C was identified as the activator of NSP4 in vivo, as cathepsin C deficiency resulted in a complete absence of NSP4 in a Papillon-Lefevre patient. Our in-depth analysis of NSP4 establishes this arginine-specific protease as a genuine member of preactivated serine proteases stored in azurophil granules of human neutrophils