The Effects of Possible Contamination on the Radiocarbon Dating of the Dead Sea Scrolls II: Empirical Methods to Remove Castor Oil and Suggestions for Redating

While kept at the Rockefeller Museum in East Jerusalem, many Dead Sea Scroll fragments were exposed to castor oil by the original team of editors in the course of cleaning the parchments. Castor oil must be regarded as a serious contaminant in relation to radiocarbon dating. If modern castor oil is present and is not removed prior to dating, the 14C dates will be skewed artificially towards modern values. Earlier, it was shown that the standard AAA pretreatment procedure used in the 2 previous studies dating Dead Sea Scroll samples is not capable of removing castor oil from parchment samples. In the present work, we show that it is unlikely that castor oil reacts with the amino acids of the parchment proteins, a finding which leaves open the possibility of devising a cleaning method that can effectively remove castor oil. We then present 3 different pretreatment protocols designed to effectively remove castor oil from parchment samples. These involve 3 different cleaning techniques: extraction with supercritical CO2, ultrasound cleaning, and Soxhlet extraction—each with their own advantages and disadvantages. Our data show that the protocol involving Soxhlet extraction is the best suited for the purpose of decontaminating the Dead Sea Scrolls, and we recommend that this protocol be used in further attempts to 14C date the Dead Sea Scrolls. If such an attempt is decided on by the proper authorities, we propose a list of Scroll texts, which we suggest be redated in order to validate the 14C dates done earlier.

Bæredygtig udvikling i det byggede miljø:Tværgående analyse af afledte effekter og dilemmaer ved bæredygtigt byggeri

Med denne rapport samles der op på både forskningsmæssige og kommercielle perspektiver på den bæredygtige forandringsproces i bygge- og ejendomsbranchen. Den igangværende transition, der kommer til at præge branchens praksisser, forretningsmodeller og output, giver lejlighed til at rejse spørgsmålet om hvilke effekter og tendenser, der allerede har og potentielt vil komme til at påvirke aktørernes ageren og spillerum

Biochemical characterization of bovine plasma thrombin-activatable fibrinolysis inhibitor (TAFI)

<p>Abstract</p> <p>Background</p> <p>TAFI is a plasma protein assumed to be an important link between coagulation and fibrinolysis. The three-dimensional crystal structures of authentic mature bovine TAFI (TAFIa) in complex with tick carboxypeptidase inhibitor, authentic full lenght bovine plasma thrombin-activatable fibrinolysis inhibitor (TAFI), and recombinant human TAFI have recently been solved. In light of these recent advances, we have characterized authentic bovine TAFI biochemically and compared it to human TAFI.</p> <p>Results</p> <p>The four N-linked glycosylation sequons within the activation peptide were all occupied in bovine TAFI, similar to human TAFI, while the sequon located within the enzyme moiety of the bovine protein was non-glycosylated. The enzymatic stability and the kinetic constants of TAFIa differed somewhat between the two proteins, as did the isoelectric point of TAFI, but not TAFIa. Equivalent to human TAFI, bovine TAFI was a substrate for transglutaminases and could be proteolytically cleaved by trypsin or thrombin/solulin complex, although small differences in the fragmentation patterns were observed. Furthermore, bovine TAFI exhibited intrinsic activity and TAFIa attenuated tPA-mediated fibrinolysis similar to the human protein.</p> <p>Conclusion</p> <p>The findings presented here suggest that the properties of these two orthologous proteins are similar and that conclusions reached using the bovine TAFI may be extrapolated to the human protein.</p

High-level secretion of native recombinant human calreticulin in yeast

Additional file 2. Elution profiles of recombinant CRT in anion-exchange chromatography. Separation of CRT from S. cerevisiae (A and B) was performed on a pre-packed 5 ml Q-Sepharose column (GE LifeSciences cat. no. 17-5156-01), equilibrated with 20 mM l-His, pH 5.5, 100 mM NaCl buffer, in 15 column volumes linear gradient from 100 mM to 500 mM NaCl. Separation of CRT from P. pastoris (C and D) was performed on a 15 ml Q-Sepharose sorbent (GE LifeSciences cat. no. 17-0510-10) packed into the XK 16/20 column (GE Lifesciences, cat. no. 28-9889-37), equilibrated with 20 mM l-His, pH 5.5, 100 mM NaCl buffer, in 10 column volumes linear gradient from 100 to 500 mM NaCl. Elution profiles (A and C) and SDS-PAGE gels of corresponding fractions (B and D) are shown. Dashed lines define fractions that were pooled and used for further experiments with purified protein