25 MBq/mu l) Avidin-tagged human islets could bind on average 2

25 MBq/mu l). Avidin-tagged human islets could bind on average 2.2% of administered tracer/mu l. Specificity (>90%) and retention (>90% after 1 h) were high for both AARs and avidin-tagged islets. Hepatic tracer uptake and retention were increased in mice transplanted with AARs [standardized uptake value (SUV)=2.6] compared to the untreated group (SUV=1.4). In vivo uptake of tracer to AARs was blocked by preadministration of unlabeled biotin.

Conclusions: Avidin-tagged islet-like objects can be tracked find more in hepatic volume after intraportal transplantation

by using [Ga-68]Ga-DOTA-(PEG)(2)-biotin and PET. (C) 2012 Elsevier Inc. All rights reserved.”
“Streptococcus suis is recognized as a major swine pathogen and an emerging zoonotic agent. Two large-scale outbreaks of severe S. suis epidemics occurred in China in 1998 and 2005 that posed serious concerns to public health and challenged the conventional conception that opportunistic

infections of S. suis serotype 2 (SS2) in humans were only sporadic cases. An extensive, collaborative study on Chinese SS2 variants, which exhibit strong invasiveness and high pathogenicity, has resulted in the description of a new disease form of streptococcal toxic shock syndrome (STSS) and a putative pathogenicity island (termed 89K). The abbreviation of STSS is used for the severe Selleckchem AICAR disease caused by both Staphylococci and Streptococci. The main virulence factors involved in STSS caused by either Staphylococcus aureus or Streptococcus pyogenes consist of so-called superantigens or molecules that trigger a nonspecific, uncontrolled activation of T cells and massive cytokine

release. However, although a collection of new virulence factors have been described, no superantigen candidates have been found for SS2 strains, implying that a different mechanism could be involved in the STSS form caused by SS2 variants.”
“Amongst the various endogenous growth factors, epidermal growth factor (EGF) plays an important role in normal wound healing of tissue such as skin, cornea and gastrointestinal already tract. Various studies have proved that supplementing recombinant human EGF (rhEGF) results in significant augmentation of wound healing. In the present work, a high level expression system with poly-arginine sequences was used for the production of recombinant human EGF (rhEGF) as inclusion bodies. The inclusion bodies were solubilized and the protein was refolded by using expanded-bed adsorption chromatography. The renatured protein was digested with appropriate concentration of trypsin and subsequently the digested rhEGF is purified by passing through ion-exchange chromatography (Toyopearl-SP) to obtain a biologically active protein.

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