Anthropic modifications on megafauna bones in the paleontological collections of the Museum national d’Histoire naturelle de Paris: Historical aspects and implications for the Pampean Pleistocene peopling

The most abundant evidence of Pampean Pleistocene human presence are modified bones, as lithic procurement sites located farther than 300 km away. Therefore, we focused on the study of bone modifications, in particular cut and percussion marks. We studied Pampean paleontological collections of Argentine and European museums as an alternative resource of previously unnoticed human modification evidences. We compared marks characteristics with those of archaeological collections from diverse climatic and cultural adaptations, from middle Pleistocene sites (Vallonet, Atapuerca, Lazaret, Arago and Terra Amata) to terminal Pleistocene ones (Abri Pataud, Isturiz and La Vache). Marks typologies were defined, leading to the identification of a particular cutmark that we named double parallel considered as highly diagnostic of anthropic use of lithic artifacts. We also propose that hafted artifacts were used on carcass processing. Perimortem bone modifications are classified in relation with mark morphology (e.g., percussion striae), inferred gesture or action (e.g., breakage of diaphysis), and inferred objective of that action (e.g., marrow extraction). The megafauna specimens analyzed from the historical collections (d’Angelis-Vilardebó, 1847, Muñiz-Dupotet, 1842 and Breton-Bonnement, 1881) present modifications compatible with dismemberment, defleshing, tongue and masseter extraction, and utilization as anvils. The lack of contextual data (location, stratigraphy) and the loss due to museum selection/collecting of accompanying material prevent paleoenvironmental and paleoecological inferences. Regional geology indicates that most of the historical collections were exhumed in riverbank cuts with ages between 70 and 13 ky BP. Preliminary direct dating presents evidence of a Pampean human occupation, at least, since OIS 2.     

Isolation and Characterization of a Cysteine Protease of Freesia Corms

A protease, freesia protease (FP)-A, was purified to electrophoretic homogeneity from regular freesia (Freesia reflacta) corms in harvest time. The M _r of FP-A was estimated to be 24 k by SDS-PAGE. The optimum pH of the enzyme was 8.0 using a casein substrate. These enzymes were strongly inhibited by p-chloromercuribenzoic acid but not by phenylmethane-sulfonylfluoride and EDTA. These results indicate that FP-A belongs to the cysteine proteases. The amino terminal sequence of FP-A was similar to that of papain, and the sequences was regarded to the conservative residues of cysteine protease. From the hydrolysis of peptidyl-pNAs, the specificity of FP-A was found to be broad. It was thought that FP-A was a new protease from freesia corms.     

Purification and Characterization of a Cysteine Protease from Corms of Freesia,Freesia reflacta

A protease (freesia protease B) has been purified to electrophoretic homogeneity from corms of freesia, Freesia reflacta by five steps of chromatography. Its M_r was estimated to be about 26,000 by SDS–PAGE. The optimum pH of the enzyme was 6.0–7.0 at 30°C using casein as a substrate. The enzyme was strongly inhibited by p-chloromercuribenzoic acid but not by phenylmethanesulphonylfluoride and EDTA. These results indicate that freesia protease B is a cysteine protease. Nine sites of oxidized insulin B-chain were cleaved by freesia protease B in 24 h of hydrolysis. The four cleavage sites among them resembled those of papain. From the digestion of five peptidyl substrates the specificity of freesia protease B was found to be approximately broad, but the preferential cleavage sites were negatively charged residues at positions. Freesia protease B preferred also the large hydrophobic amino acid residues at the P₂ position, in a similar manner to papain. The amino terminal sequence of freesia protease B was identical with those of papain in regard to the conservative residues of cysteine protease.     

Daffodil flowers delay senescence in cut Iris flowers

Visible symptoms of tepal senescence in cut Iris x hollandica (cv. Blue Magic) flowers were delayed by placing one cut daffodil flower (Narcissus pseudonarcissus, cv. Carlton) in the same vase. Addition of mucilage, exuded by daffodil stems, to the vase water had the same effect as the flowering daffodil stem. The active compound in the mucilage was identified as narciclasine (using LC/MS, GC/MS, 1H and 13C-NMR, and comparison with an authentic sample of narciclasine). The delay of senescence, either by mucilage or purified narciclasine, was correlated with a delayed increase in protease activity, and with a considerable reduction of maximum protease activity. Narciclasine did not affect in vitro protease activity, but is known to inhibit protein synthesis at the ribosomal level. Its effects on senescence and protease activity were similar to those of cycloheximide (CHX), another inhibitor of protein synthesis, but the effective narciclasine concentration was about 100 times lower than that of CHX. It is concluded that the delay of Iris tepal senescence by daffodil stems is due to narciclasine in daffodil mucilage, which apparently inhibits the synthesis of proteins involved in senescence.     

表油菜素内酯对月季切花保鲜作用的研究

本文初步探讨了表油菜素内酯（epiBR）对瓶插月季切花的保鲜作用。与对照（蒸馏水）和基本液（2％蔗糖＋500mgL-1柠檬酸＋250mgL-8-羟基喹啉＋25mgAgNO3）相比,经epiBR处理（基本液＋0．1mgL-1epiBR）的月季切花花枝坚挺,蓝变延迟,瓶插寿命延长1-1.5倍。测定有关生理指标表明,epiBR处理对月季切花瓶插花枝前期鲜重的增加及后期的保持有明显作用。并显著延缓花瓣和叶片质膜相对透性的增加,还能使瓶插前期花瓣还原糖含量增加。epiBR处理对花瓣蛋白质和叶片叶绿素含量变化无明显影响,而对花瓣花青素水平下降有轻微的促进作用。     

1-MCP-β-环糊精对香石竹切花保鲜作用的研究

对香石竹切花(Dianthus caryophyllus L.)用不同体积浓度的1-MCP-β-环糊精溶液处理不同的时间,观察其外观形态品质和生理生化指标,得知以50 mg/L的1-MCP-β-环糊精溶液在7 m³的密闭体系中处理8 h效果最佳。能极大提高香石竹切花的观赏价值,减少萎蔫程度,延缓开放,延迟香石竹切花叶片质膜相对透性下降,并对叶片叶绿素含量变化有一定的影响。     

Analysis of low molecular weight plasma proteins using ultrafiltration and large gel two‐dimensional electrophoresis

In this study, various solvent systems were applied to obtain a high and consistent recovery rate of low molecular weight plasma proteins (LMPP) from human plasma. A buffer system containing 7 M urea, 2 M thiourea, 25 mM NH₄HCO₃ + 20% ACN (pH 8.2) produced the highest recovery rate of LMPP. To validate the recovery of cut off membrane (COM) obtained using the urea buffer system, 27 different 30 kDa COMs were used to prepare the LMPP sample which were then subjected to 1‐D SDS‐PAGE. Statistical analysis showed that the buffer system with COM produced a consistent the recovery of LMPP. In addition, 2‐DE analysis was also conducted to determine the relative intensity of each protein spot. When molecular weight ranges over 30 kDa and under 30 kDa were evaluated, 953 and 587 protein spots were observed in the gels, respectively, resulting in a total of 1540 protein spots being resolved. Identification of the major proteins were then performed using a nano‐LC/MS system comprised of an HPLC system and an ESI‐quadrupole IT MS equipped with a nano‐ESI source.