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112 records – page 1 of 12.

Acoustic emission during cooling and heating of aqueous solutions of polyethylene glycols of molecular masses from 300 to 3000.

https://arctichealth.org/en/permalink/ahliterature9640
Source
Cryobiology. 2003 Aug;47(1):40-3
Publication Type
Article
Date
Aug-2003
Author
A V Zinchenko
V D Zinchenko
Author Affiliation
Institute for Problems of Cryobiology and Cryomedicine of the National Academy of Sciences of Ukraine, 23 Pereyaslavskaya str., Kharkov 61015, Ukraine. cryo@online.kharkov.ua
Source
Cryobiology. 2003 Aug;47(1):40-3
Date
Aug-2003
Language
English
Publication Type
Article
Keywords
Acoustics - instrumentation
Cold
Cryopreservation
Crystallization
Heat
Molecular Weight
Polyethylene Glycols - chemistry
Solutions - chemistry
Water - chemistry
Abstract
The object of this research is to study acoustic emissions (AE) in aqueous solutions of polyethylene glycols (PEGs) of molecular masses from 300 to 3000 during cooling at 100 degrees C/min and heating at 70 degrees C/min in the temperature range from 0 to -196 degrees C. The dependence of AE intensity on PEG concentration and molecular mass is analysed. The AE intensity correlated with the crystalline to amorphous phase ratio in the frozen system.
PubMed ID
12963411 View in PubMed
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[Activity of carbohydratephosphate metabolism enzymes in liver slices after freezing and thawing]

https://arctichealth.org/en/permalink/ahliterature13160
Source
Ukr Biokhim Zh. 1977 May-Jun;49(3):10-5
Publication Type
Article
Author
V I Lugovii
L I Zolochevs'ka
A M Dziuba
Source
Ukr Biokhim Zh. 1977 May-Jun;49(3):10-5
Language
Ukrainian
Publication Type
Article
Keywords
Animals
Drug Stability
English Abstract
Freezing
Glucosephosphate Dehydrogenase - metabolism
Hexokinase - metabolism
L-Lactate Dehydrogenase - metabolism
Liver - drug effects - enzymology
Phosphorylases - metabolism
Polyethylene Glycols - pharmacology
Rats
Subcellular Fractions - enzymology
Abstract
Activity of hexokinase, phosphorylase, glucoso-6-phosphate dehydrogenase lactate-dehydrogenase was studied in liver slices, homogenate and supernatant fraction after freezing at a rate of 1 degree/min down to -30 degrees C. The enzyme activity in homogenate and supernatant fraction does not change after freezing. A significant reduction in the activity of most enzymes that is followed by an increase in their activity in the freezing medium was observed in the experiments. Cryoprotectant polyethylene glycol, mol. wt. 300 and 1,000 (PEG-300 and PEG-1,000), partially prevents the observed changes in the enzyme activity; PEG-1,000 is more effective than PEG-300. Experimental results show that the main reason for the reduction of the enzyme activity observed after freezing the tissue slices is a decrease in the volume of intracellular enzyme proteins due to their leakage from the injured cellular elements into the exocellular medium.
PubMed ID
888219 View in PubMed
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Activity of lysosomal enzymes in the bile and serum of mice with intrahepatic cholestasis.

https://arctichealth.org/en/permalink/ahliterature90427
Source
Bull Exp Biol Med. 2008 May;145(5):560-3
Publication Type
Article
Date
May-2008
Author
Korolenko T A
Savchenko N G
Yuz'ko Ju V
Alexeenko T V
Sorochinskaya N V
Author Affiliation
Institute of Physiology, Siberian Division of the Russian Academy of Medical Sciences, Novosibirsk, Russia. t.a.korolenko@iph.ma.nsc.ru
Source
Bull Exp Biol Med. 2008 May;145(5):560-3
Date
May-2008
Language
English
Publication Type
Article
Keywords
1-Naphthylisothiocyanate - toxicity
Alkaline Phosphatase - blood - metabolism
Animals
Bile - enzymology
Cholestasis, Intrahepatic - blood - chemically induced - enzymology
Cholesterol - biosynthesis - blood
Hexosaminidases - blood - metabolism
Lysosomes - enzymology
Male
Mice
Mice, Inbred CBA
Polyethylene Glycols - toxicity
beta-Galactosidase - blood - metabolism
beta-N-Acetylhexosaminidases - blood - metabolism
gamma-Glutamyltransferase - blood - metabolism
Abstract
Lysosomal enzyme activity in the bile and blood serum was compared in mice with experimental intrahepatic cholestasis induced by alpha-naphthyl isothiocyanate and Triton WR 1339. Triton WR 1339 increases the synthesis of cholesterol (fatty acid precursor) in liver cells. The development of intrahepatic cholestasis was confirmed by the increase in activities of alkaline phosphatase and gamma-glutamyltransferase in blood serum. Administration of Triton WR 1339 in a dose of 100 mg/100 g was followed by a 10-fold increase in beta-galactosidase activity (hepatocyte lysosomal enzyme) in the bile, but not in the serum of mice. beta-Galactosidase activity significantly increased in the bile, but decreased in the serum of mice after treatment with a-naphthyl isothiocyanate in a dose of 200 mg/kg. Our results indicate that intrahepatic cholestasis is manifested in increased secretion of lysosomal glycosidases into the bile. Bile components can aggravate damage to liver cells by affecting the processes of hepatocyte apoptosis and necrosis.
PubMed ID
19145281 View in PubMed
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An improved method for the purification of IgG monoclonal antibodies from culture supernatants.

https://arctichealth.org/en/permalink/ahliterature11823
Source
J Immunol Methods. 1992 Oct 19;155(1):129-32
Publication Type
Article
Date
Oct-19-1992
Author
D A Brooks
T M Bradford
J J Hopwood
Author Affiliation
Department of Chemical Pathology, Adelaide Medical Centre for Women and Children, Australia.
Source
J Immunol Methods. 1992 Oct 19;155(1):129-32
Date
Oct-19-1992
Language
English
Publication Type
Article
Keywords
Ammonium Sulfate
Animals
Antibodies, Monoclonal
Cells, Cultured
Chondro-4-Sulfatase - immunology
Culture Media
Dialysis
Electrophoresis, Polyacrylamide Gel
Enzyme-Linked Immunosorbent Assay
Hybridomas - immunology
Immunoglobulin G - isolation & purification
Methods
Mice
Polyethylene Glycols
Precipitation
Research Support, Non-U.S. Gov't
Abstract
A method for the purification of mouse monoclonal antibodies from hybridoma culture supernatants is described. The protocol involves the use of a combination of three previously described methods for the concentration and purification of monoclonal antibodies. Firstly, hybridomas were grown in a Diacult dialysis system (Inter Med Laboratory, Denmark) to yield milligram quantities of monoclonal antibody in a culture supernatant. Monoclonal antibodies were then purified from the culture supernatant by precipitation with polyethylene glycol 6000 (PEG 6000) and finally reprecipitated using an ammonium sulphate procedure. The PEG 6000 treatment caused a density change in the ammonium sulphate immunoglobulin precipitate, and resulted in the formation of a pellicle which contained pure mouse monoclonal antibody. The protocol removed contaminating bovine serum immunoglobulin as well as other serum and cellular protein from the monoclonal antibody preparations.
PubMed ID
1401962 View in PubMed
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An intraluminal prosthesis may improve healing of a one-layer colonic anastomosis: an experimental study in pigs.

https://arctichealth.org/en/permalink/ahliterature9924
Source
Eur J Surg. 2002;168(3):165-71
Publication Type
Article
Date
2002
Author
N. Buch
H. Glad
P. Svendsen
H R Witek Oxlund
F. Gottrup
C P Hovendal
Source
Eur J Surg. 2002;168(3):165-71
Date
2002
Language
English
Publication Type
Article
Keywords
Anastomosis, Surgical - methods
Animals
Colon - surgery
Female
Intubation - instrumentation
Polyethylene Glycols
Postoperative Complications
Prosthesis Implantation
Swine
Wound Healing
Abstract
OBJECTIVE: To compare healing of one-layer colonic anastomoses with or without a soluble intraluminal prosthesis (* SBS-tube). DESIGN: Randomised, partly blinded controlled study. SETTING: University hospital, Denmark. SUBJECTS: 16 female Danish country strain pigs, of which 8 had the SBS tube inserted and 8 acted as controls. INTERVENTIONS: One-layer colonic anastomoses either hand-sewn (n = 8, controls) or hand-sewn onto an SBS tube (n = 8). MAIN OUTCOME MEASURES: Macroscopic evaluation, leakage test, breaking strength, histology, oxygen tension in and near the anastomosis peroperatively and 4 days postoperatively. RESULTS: Three quarters of the tubes (n = 8) dissolved in less than 2 hours. Histological examination showed significantly better structured layers and more mucosal epithelial covering in the SBS group. The other histological variables examined were: tissue gap (p
PubMed ID
12182242 View in PubMed
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[Antiviral therapy of chronic hepatitis C: 30 years success story].

https://arctichealth.org/en/permalink/ahliterature305446
Source
Ter Arkh. 2019 Nov 15; 91(11):110-115
Publication Type
Journal Article
Date
Nov-15-2019
Author
D T Abdurakhmanov
T P Rozina
E N Nikulkina
E Z Burnevich
E L Tanashuk
M V Severov
A L Filatova
S Y Milovanova
V V Karpov
S V Moiseev
Author Affiliation
Tareev Clinic of Rheumatology Nephrology and Occupational Disease Sechenov First Moscow State Medical University.
Source
Ter Arkh. 2019 Nov 15; 91(11):110-115
Date
Nov-15-2019
Language
Russian
Publication Type
Journal Article
Keywords
Antiviral agents - therapeutic use
Drug Therapy, Combination
Hepacivirus
Hepatitis C - drug therapy
Hepatitis C, Chronic - drug therapy
Humans
Polyethylene Glycols - therapeutic use
Recombinant Proteins - therapeutic use
Ribavirin - therapeutic use
Russia
Abstract
Exactly 30 years ago, hepatitis C virus was identified. Over the years, tremendous success has been achieved in the treatment of hepatitis C, which is currently considered to be an almost completely curable disease. The review presents the main stages in the development of hepatitis C antiviral therapy, the efficacy of various treatment regimens. The greatest progress in treatment was noted over the past 5 years when drugs with direct antiviral action appeared and began to be widely used, including in Russia, which ensure the elimination of the virus in 90-95% of cases.
????? 30 ??? ????? ??? ??????????????? ????? ???????? ?. ?? ??? ???? ????????? ???????? ????? ? ??????? ???????? ?, ??????? ? ????????? ????? ??????????????? ??? ??????????? ????????? ????????? ???????????. ? ?????? ???????????? ???????? ????? ??????????? ??????????????? ??????? ???????? ?, ????????????? ????????? ???? ???????. ?????????? ???????? ? ??????? ??????? ? ??????? ????????? 5 ???, ????? ????????? ? ????? ?????? ???????????, ? ??? ????? ? ? ??????, ????????? ? ?????? ??????????????? ?????????, ??????? ???????????? ?????????? ?????? ? 90-95% ???????.
PubMed ID
32598621 View in PubMed
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Apoptosis induced by the monomers HEMA and TEGDMA involves formation of ROS and differential activation of the MAP-kinases p38, JNK and ERK.

https://arctichealth.org/en/permalink/ahliterature82868
Source
Dent Mater. 2007 Jan;23(1):34-9
Publication Type
Article
Date
Jan-2007
Author
Samuelsen Jan T
Dahl Jon E
Karlsson Stig
Morisbak Else
Becher Rune
Author Affiliation
NIOM-Nordic Institute of Dental Materials, PO Box 70, N-1305 Haslum, Norway. jts@niom.no
Source
Dent Mater. 2007 Jan;23(1):34-9
Date
Jan-2007
Language
English
Publication Type
Article
Keywords
Animals
Antioxidants - pharmacology
Apoptosis - drug effects
Ascorbic Acid - pharmacology
Blotting, Western
Caspases - metabolism
Cell Line
Dental Materials - pharmacology
Enzyme Activation - drug effects
Flavonoids - pharmacology
Fluorescent Dyes - diagnostic use
MAP Kinase Kinase 4 - antagonists & inhibitors - metabolism
Methacrylates - pharmacology
Mitogen-Activated Protein Kinases - antagonists & inhibitors - metabolism
Polyethylene Glycols - pharmacology
Polymethacrylic Acids - pharmacology
Rats
Reactive Oxygen Species - metabolism
Signal Transduction - drug effects
Time Factors
p38 Mitogen-Activated Protein Kinases - antagonists & inhibitors - metabolism
Abstract
OBJECTIVES: Cytotoxic methacrylate monomers have been identified in aqueous extracts of freshly cured compomers. Some of these compounds, including HEMA and TEGDMA, induce apoptosis and necrosis in vitro. The aim of the present study was to elucidate possible signaling pathways involved in apoptosis following exposure to HEMA or TEGDMA in a salivary gland cell line. METHODS: The cells were exposed to various concentrations of HEMA or TEGDMA. ROS formation was determined by dichlorofluorescein assay. Phosphorylated MAP-kinases ERK1/2, p38 and JNK, as well as specific caspases were identified by Western blotting. Apoptosis was assayed by fluorescence microscopy. RESULTS: HEMA or TEGDMA exposure resulted in ROS formation and concentration-dependent apoptosis as well as phosphorylation of ERK. Phosphorylation of JNK and p38 was induced by HEMA. Selective inhibitors of ERK and JNK modified the apoptotic response after HEMA and TEGDMA exposure, whereas p38 inhibition modified the apoptotic response only after HEMA exposure. Vitamin C reduced HEMA-induced apoptosis. SIGNIFICANCE: ROS formation and differential MAP kinase activation appear to be involved in the apoptotic response following exposure to HEMA and TEGDMA.
PubMed ID
16430953 View in PubMed
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Autologous and homologous fibrinogen sealants: adhesive strength.

https://arctichealth.org/en/permalink/ahliterature12299
Source
Laryngoscope. 1989 Sep;99(9):974-6
Publication Type
Article
Date
Sep-1989
Author
K. Laitakari
J. Luotonen
Author Affiliation
Department of Otolaryngology, University of Oulu, Finland.
Source
Laryngoscope. 1989 Sep;99(9):974-6
Date
Sep-1989
Language
English
Publication Type
Article
Keywords
Adhesiveness
Animals
Aprotinin
Comparative Study
Drug Combinations
Factor XIII
Fibrin Tissue Adhesive
Fibrinogen
Humans
Polyethylene Glycols
Rats
Thrombin
Tissue Adhesives
Abstract
The adhesive strength of autologous fibrinogen sealants prepared from the individual patient's blood with the help of ammonium sulphate or polyethylene glycol was compared to that of a homologous commercial fibrinogen sealant. The concentration of the fibrinogen harvested by each method was measured. The bonding power measurements were carried out by gluing pieces of human dura, rat skin, or cotton cloth together. The commercial fibrinogen sealant yielded the highest concentration of fibrinogen and also proved to be the strongest of the glues tested. The PEG glue was better than the AS glue. Humidity did not have a significant influence on adhesive strength, nor did deep-freezing worsen the properties of the fibrinogen sealants. In addition to the commercial products, the self-made fibrinogen glues, especially the PEG glue, were also strong enough for otolaryngological use.
PubMed ID
2475731 View in PubMed
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Can nutritional supplements and rectal enema be used as bowel cleansing for colonoscopy?--Results of a randomized controlled pilot study.

https://arctichealth.org/en/permalink/ahliterature258315
Source
Scand J Gastroenterol. 2014 Apr;49(4):485-91
Publication Type
Article
Date
Apr-2014
Author
Ulf O Gustafsson
Josefin Segelman
Olle Ljungqvist
Anders Thorell
Jonas Nygren
Author Affiliation
Department of surgery, Ersta Hospital & Department of Clinical Sciences, Danderyd Hospital, Karolinska Institutet , Stockholm , Sweden.
Source
Scand J Gastroenterol. 2014 Apr;49(4):485-91
Date
Apr-2014
Language
English
Publication Type
Article
Keywords
Adult
Aged
Aged, 80 and over
Colonoscopy
Dietary Proteins - therapeutic use
Enema
Female
Humans
Male
Middle Aged
Pilot Projects
Polyethylene Glycols - therapeutic use
Sweden
Abstract
Currently available preparations for colonoscopy have low tolerability and may cause fluid and electrolyte shifts. An alternative method of bowel cleansing is required.
Preparation of the gut using oral nutritional supplements (ONS) and rectal enema was tested as an alternative method of bowel cleansing. During 2008-2012, patients were randomized to oral nutritional supplements (n = 27) for 5 days and rectal enema or polyethylene glycol (PEG) (n = 23) prior to colonoscopy. Blinded endoscopists rated the degree of bowel cleansing according to the Ottawa bowel preparation scale (OBS) (primary outcome). Tolerability of either preparation was also assessed (ClinicalTrials.gov. Identifier no: NCT00123456).
Due to a high rate of bowel cleansing failure among patients receiving ONS, the study was interrupted prematurely. Colonoscopies were incomplete due to stools in 6 of 27 patients in the ONS group compared to 1 of 23 in the PEG group (ns). The mean total OBS were 8.3 ± 3.3 and 5.3 ± 2.8, respectively (p = 0.002). Four patients (15%) in the ONS group and eight patients (35%) receiving PEG had an OBS score =4 (good preparation) (ns). ONS was better tolerated than PEG with more patients reporting acceptable taste (27 of 27 [100%] vs. 15 of 23 [65%], p = 0.001), and fewer reporting difficulties with the intake (0 of 27 [0%] vs. 10 of 23 [43%], p
PubMed ID
24495046 View in PubMed
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Cell surface proteins of encapsulated Streptococcus cremoris: identification and immunochemical characterization.

https://arctichealth.org/en/permalink/ahliterature12573
Source
J Appl Bacteriol. 1987 Aug;63(2):133-7
Publication Type
Article
Date
Aug-1987
Author
S. Kontusaari
R. Forsén
Author Affiliation
Department of Biochemistry, University of Oulu, Finland.
Source
J Appl Bacteriol. 1987 Aug;63(2):133-7
Date
Aug-1987
Language
English
Publication Type
Article
Keywords
Animals
Antigens, Bacterial - analysis
Detergents
Electrophoresis, Polyacrylamide Gel
Hydrogen-Ion Concentration
Immunoassay
Milk - microbiology
Octoxynol
Polyethylene Glycols
Research Support, Non-U.S. Gov't
Streptococcus - immunology
Abstract
Cell surface proteins of two slime-forming, encapsulated Streptococcus cremoris strains, MLS96 and T5 from the fermented milk product viili, were extracted with the non-ionic detergent Triton X-100. The isolated protein antigens were characterized by sodium dodecyl sulphate polyacrylamide gel electrophoresis and immunoblotting with antisera produced against whole Strep. cremoris cells. When protein profiles of these strains were compared, seven prominent polypeptides were found common to both and were recognized by both antisera. Five of these polypeptides with molecular weights of 70,000, 54,000, 50,000, 47,000 and 40,000 were identified as cell wall components. The remaining two polypeptides with molecular weights of 42,000 and 26,000 are being studied further in connection with slime formation for which modified Triton X-100 extraction provides a suitable method for isolation of the surface-associated antigens of lactic streptococci.
PubMed ID
3654403 View in PubMed
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112 records – page 1 of 12.