ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTPreparation of 1-Indanones from α-Bromoaralkyl Ketones1ROBERT W. LAYER and IAN R. MacGREGORCite this: J. Org. Chem. 1956, 21, 10, 1120–1123Publication Date (Print):October 1, 1956Publication History Published online1 May 2002Published inissue 1 October 1956https://pubs.acs.org/doi/10.1021/jo01116a017https://doi.org/10.1021/jo01116a017research-articleACS PublicationsRequest reuse permissionsArticle Views205Altmetric-Citations7LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts
A two-site sandwich ELISA was developed to measure PAI-1 antigen and utilised a polyclonal antiserum produced against PAI-1 purified from human endothelial cell secretory products. The assay was calibrated against a preparation of pure PAI-1 whose protein concentration had been determined by amino acid analysis and the detection limit was 30 pg PAI-1 ml-1 sample. PAI-1 was detected in primate sera but not in a wide range of non-primate sera and no cross-reactivity with alpha 2-antiplasmin or antithrombin III was observed. The ELISA was used to study cellular secretion of PAI-1 which was confirmed as a major secretory protein in human umbilical vein endothelial cells (HUVEC). PAI-1 antigen accumulated in the medium in a linear fashion with time and accounted for approximately equal to 10% of total secreted protein. Specific activity of intracellular PAI-1 was typically 20-fold greater than that of PAI-1 in 24 h conditioned medium and a t1/2 for inactivation of secreted PAI-1 of 0.53 h was calculated. Purified endotoxin stimulated the secretion of PAI-1 antigen and raised the intracellular levels in HUVEC cultures showing that the anti-fibrinolytic actions of endotoxin are effected by increasing the rate of synthesis and secretion of PAI-1.
Variant CJD (vCJD) is an incurable, infectious human disease, likely arising from the consumption of BSE-contaminated meat products. Whilst the epidemic appears to be waning, there is much concern that vCJD infection may be perpetuated in humans by the transfusion of contaminated blood products. Since 2004, several cases of transfusion-associated vCJD transmission have been reported and linked to blood collected from pre-clinically affected donors. Using an animal model in which the disease manifested resembles that of humans affected with vCJD, we examined which blood components used in human medicine are likely to pose the greatest risk of transmitting vCJD via transfusion. We collected two full units of blood from BSE-infected donor animals during the pre-clinical phase of infection. Using methods employed by transfusion services we prepared red cell concentrates, plasma and platelets units (including leucoreduced equivalents). Following transfusion, we showed that all components contain sufficient levels of infectivity to cause disease following only a single transfusion and also that leucoreduction did not prevent disease transmission. These data suggest that all blood components are vectors for prion disease transmission, and highlight the importance of multiple control measures to minimise the risk of human to human transmission of vCJD by blood transfusion.
Human peripheral blood neutrophils were exposed in vitro, in a tonometer, to two different fractions of cigarette smoke–designated particulate phase and vapor phase. The proteolytic activity of the cells following exposure was assessed by measuring their elastase release and ability to degrade fibronectin. At levels of smoke exposure that were physiologically attainable, neither smoke fraction caused an increase in elastase release or fibronectin degradation. In most experiments, fibronectin proteolysis was suppressed by smoke exposure–an effect that was reversible on treatment with phorbol myristate acetate. These data provide evidence that the proteolytic activity of neutrophils is not enhanced by a direct effect of cigarette smoke on these cells.
Summary. Aqueous solutions of stroma‐free human haemoglobin are being evaluated as potential oxygen‐carrying resuscitation fluids. There are indications, however, that such solutions may produce toxic side‐effects in vivo. Stroma‐free haemoglobin solution produced a 50% fall in mean arterial pressure when infused into a small animal model despite containing very low levels of non‐haem protein and phospholipid contaminants. This effect was not produced by haemoglobin solutions after extensive dialysis. Red cell‐derived adenine nucleotides were found to be present in concentrations high enough to cause such a response (80–85 μg/ml). We have developed a chromatographic assay capable of predicting hypotension in our animal model and consider that the complete absence of adenine nucleotides must be confirmed in all studies concerning the possible toxic side‐effects of stroma‐free haemoglobin solutions.
Studies using a time‐resolved fluoroimmuno‐assay (DELFIA®) have shown that platelets and plasma are the main compartments of the normal isoform of prion protein (PrP c ) in human blood. The aim of the present study was to monitor PrP c levels in various fractions of apheresis platelet concentrates (PC) during storage and to assess the association of this release with α granule protein β‐thrombo‐globulin (BTG) and cytoplasmic lactate dehydrogenase (LDH) as cell activation and cell lysis markers, respectively. Six apheresis PC were obtained from volunteer donors using Haemonetics MCS and stored up to 10 days. 7–9 mL samples were aseptically collected from each PC on days 1, 2, 3, 4, 5, 8, and 10 of storage. Platelet poor plasma (PPP) and platelets (P) were prepared and the PPP split into two equal fractions, one of which was centrifuged at 40,000g for 2 h at 4 °C to remove microparticles (MP) [high spun plasma (HSP)]. The results showed that the mean overall levels of PrP c during storage remained within 15% of day 1 levels. In contrast, the mean levels in P significantly decreased to 46% day 1 levels by day 10 of storage ( P < 0·01), while the corresponding levels in plasma significantly rose by up to 329% ( P < 0·01). Moreover, although MP‐bound PrP c was released during storage, it was increasingly superceded by soluble prion protein. PrP c and BTG release exhibited very similar patterns, both showing a significant rise in PPP and HSP ( P < 0·01). In contrast, LDH showed a significant rise in HSP only towards the end of the storage period ( P < 0·01). These results indicate that PrP c is released from platelets during storage of PCs and that this release is probably due mainly to platelet activation and α‐granule release in the first few days of storage. The release of PrP c is apparently reinforced through cell lysis, and is increasingly comprised of soluble prion proteins, at longer storage periods.
In a group of six normal male volunteers, infusion of DDAVP, venous occlusion and exercise were shown to increase plasma levels of factor VIII and plasminogen activator, activity and antigen, to different extents and at differing rates. Any mechanisms suggested to explain release of these proteins by various stimuli should account for such differences. All three stimuli could also increase plasma levels of prostacyclin metabolites, although this was only significant for high doses of DDAVP. Other potential endothelial markers, such as fibronectin and thrombospondin, showed no specific increase after any of the stimuli.
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTDetermination of Monomer in Partially Polymerized Acrylic and Allyl EstersC. E. Albertson and I. R. MacGregorCite this: Anal. Chem. 1950, 22, 6, 806–809Publication Date (Print):June 17, 1950Publication History Published online1 May 2002Published inissue 17 June 1950https://pubs.acs.org/doi/10.1021/ac60042a019https://doi.org/10.1021/ac60042a019research-articleACS PublicationsRequest reuse permissionsArticle Views169Altmetric-Citations4LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts
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