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53 records – page 1 of 6.

Allergenic and immunogenic components of house dust mite, Dermatophagoides farinae.

https://arctichealth.org/en/permalink/ahliterature3845
Source
Ann Allergy. 1986 Feb;56(2):150-5
Publication Type
Article
Date
Feb-1986
Author
S. Nakada
M. Haida
T. Nakagawa
K. Ito
T. Miyamoto
Source
Ann Allergy. 1986 Feb;56(2):150-5
Date
Feb-1986
Language
English
Publication Type
Article
Keywords
Allergens
Animals
Antibodies, Anti-Idiotypic - analysis
Asthma - blood - immunology
Chromatography, Gel
Enzyme-Linked Immunosorbent Assay
Humans
Immunoglobulin G - immunology
Mice
Mice, Inbred BALB C
Mites - immunology
Research Support, Non-U.S. Gov't
Skin Tests
Tissue Extracts - isolation & purification
Abstract
The house dust mite, Dermatophagoides farinae, was fractionated by a Sephadex G-200 column. Its allergenic (IgE-reacting) and immunogenic (IgG-reacting) components were investigated. By means of skin test, the molecular weight (MW) of major allergenic components of mite was found to be approximately 9,000 to 21,000 daltons. Immunogenic components were investigated by enzyme linked immunosorbent assay using each fraction as an antigen and mice plasma and human serum as antibodies. With mouse plasma, high IgG antibody titers were observed in fractions that contained the part of the mite with high MW (greater than 150,000). With human sera, high IgG antibody titers were observed in fractions that contained the part of the mite with MW more than 30,000. Heterogeneity of human IgG antibody responses against mite antigen was also suggested.
PubMed ID
3484919 View in PubMed
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alpha-Neoendorphin-like immunoreactivity in medullary carcinoma of the thyroid.

https://arctichealth.org/en/permalink/ahliterature26178
Source
Cancer. 1987 Jan 15;59(2):277-80
Publication Type
Article
Date
Jan-15-1987
Author
M. Ohashi
T. Yanase
N. Fujio
H. Ibayashi
M. Kinjo
H. Matsuo
Source
Cancer. 1987 Jan 15;59(2):277-80
Date
Jan-15-1987
Language
English
Publication Type
Article
Keywords
Adolescent
Adult
Carcinoma - analysis
Chromatography, Gel
Endorphins - analysis
Female
Humans
Molecular Weight
Protein Precursors - analysis
Radioimmunoassay
Research Support, Non-U.S. Gov't
Thyroid Neoplasms - analysis
Abstract
alpha-Neoendorphin-like immunoreactivities (alpha-NE-IR) were demonstrated in tissues from three patients with medullary carcinoma of the thyroid (MCT). A large amount of alpha-NE-IR was detected in the extracts of primary tumors and metastatic lymphatic tissues by a highly sensitive and specific radioimmunoassay (RIA). Gel filtration analyses showed two different molecular-weight forms of the alpha-NE-IR: One eluted at the void fraction and the other at the position of [125I]-alpha-NE on Sephadex (Pharmacia Fine Chemical, Uppsala, Sweden) G-50 chromatography. Immunohistochemical examination revealed the presence of alpha-NE-IR in the C-cell carcinoma. These data presumably reflect that alpha-NE, the opioid peptide derived from preproenkephalin B, is synthesized in the MCT.
PubMed ID
3802014 View in PubMed
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Assay for cross-linked carboxyterminal telopeptide of type I collagen (ICTP) unlike CrossLaps assay reflects increased pathological degradation of type I collagen in rheumatoid arthritis.

https://arctichealth.org/en/permalink/ahliterature13868
Source
Clin Chem Lab Med. 2003 Aug;41(8):1038-44
Publication Type
Article
Date
Aug-2003
Author
Mirja-Liisa Sassi
Sari Aman
Markku Hakala
Reijo Luukkainen
Juha Risteli
Author Affiliation
Department of Clinical Chemistry, University of Oulu, Oulu, Finland.
Source
Clin Chem Lab Med. 2003 Aug;41(8):1038-44
Date
Aug-2003
Language
English
Publication Type
Article
Keywords
Adult
Aged
Arthritis, Rheumatoid - metabolism
Chromatography, Gel
Collagen - analysis - blood
Collagen Type I - metabolism
Comparative Study
Data Interpretation, Statistical
Enzyme-Linked Immunosorbent Assay
Female
Humans
Male
Middle Aged
Peptide Fragments - analysis - blood
Procollagen - analysis - blood
Radioimmunoassay
Research Support, Non-U.S. Gov't
Rheumatoid Factor - analysis - immunology
Synovial Fluid - chemistry
Abstract
We compared the ability of assay for cross-linked carboxyterminal telopeptide of type I collagen (ICTP) and CrossLaps assay to reflect increased pathological degradation of type I collagen in serum and synovial fluid samples of patients with rheumatoid arthritis (RA; n = 40). ICTP and CrossLaps concentrations were correlated with each other and with markers of collagen synthesis (PINP and PIIINP, amino terminal propeptides of type I and type III procollagens, respectively) and with markers of inflammation, i.e., C-reactive protein (CRP) and erythrocyte sedimentation rate (ESR). Serum ICTP was increased in half of the RA patients, whereas CrossLaps assays were increased only occasionally. Serum ICTP correlated with the other markers of collagen metabolism as well as with CRP and ESR. Serum CrossLaps correlated only with PINP and ICTP, but not with serum PIIINP, CRP or ESR. Two patients had false-positive reactions in the CrossLaps assay due to the rheumatoid factor. The ICTP and CrossLaps antigens were clearly separate peaks in gel filtration analysis. The CrossLaps assay is able to detect the same ICTP antigen, but not vice versa. The ICTP assay reflects increased matrix metalloproteinase-mediated collagen degradation in joints in RA. In contrast, the physiological cathepsin K-mediated bone resorption measured by the CrossLaps assay was only occasionally increased.
PubMed ID
12964811 View in PubMed
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Biochemical markers of pollutant responses in macrozoobenthos from the White Sea: intracellular proteolysis.

https://arctichealth.org/en/permalink/ahliterature258986
Source
Mar Environ Res. 2014 May;96:38-44
Publication Type
Article
Date
May-2014
Author
Liudmila Lysenko
Nadezda Kantserova
Elena Käiväräinen
Marina Krupnova
Galina Shklyarevich
Nina Nemova
Source
Mar Environ Res. 2014 May;96:38-44
Date
May-2014
Language
English
Publication Type
Article
Keywords
Amphipoda - drug effects
Animals
Biological Markers - metabolism
Chromatography, Gel
Environmental Exposure
Environmental monitoring
Mytilus edulis - drug effects
Oceans and Seas
Peptide Hydrolases - metabolism
Proteolysis - drug effects
Russia
Species Specificity
Water Pollutants, Chemical - toxicity
Abstract
Coastal environments of Kandalaksha Gulf in the White Sea (Russia) despite nature conservation efforts are heavily influenced by human activities. Biological effects of complex environmental pollution, including organic substances, heavy metals, and oil hydrocarbons, were assessed in widely distributed marine invertebrates, Gammarus duebeni (Crustacea, Amphipoda) and Mytilus edulis (Mollusca, Bivalvia), collected from a series of anthropogenically-impacted areas and distanced reference sites in Kandalaksha Gulf. The parameters of intracellular protein degradation pathways such as cytosol calpain system and lysosomal cathepsins B (CatB) and cathepsin D (CatD) were studied. The response reactions observed in invertebrates vary in specificity and ranged from adaptive to destructive depending on the total contaminant level and the nature of predominant pollutant. The ecological relevance of studied parameters as biomarkers was confirmed by their ability to indicate both expose to pollutants and adverse effects at the organism level.
PubMed ID
24559608 View in PubMed
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Brominated flame retardants and phenolic endocrine disrupters in Finnish human adipose tissue.

https://arctichealth.org/en/permalink/ahliterature183542
Source
Chemosphere. 2003 Dec;53(9):1123-30
Publication Type
Article
Date
Dec-2003
Author
Annika Smeds
Pekka Saukko
Author Affiliation
Department of Organic Chemistry, Abo Akademi University, Biskopsgatan 8, FIN-20500 Turku, Finland. ansmeds@abo.fi
Source
Chemosphere. 2003 Dec;53(9):1123-30
Date
Dec-2003
Language
English
Publication Type
Article
Keywords
Adipose Tissue - chemistry
Adolescent
Adult
Aged
Aged, 80 and over
Chromatography, Gel
Female
Finland
Flame Retardants - analysis
Gas Chromatography-Mass Spectrometry
Humans
Hydrocarbons, Brominated - analysis
Male
Middle Aged
Phenols - analysis
Abstract
Brominated flame retardants and phenolic compounds, of which several have been shown to exhibit endocrine disrupting effects, were screened in extracts of Finnish human adipose tissue samples. The samples were collected during autopsy from 39 subjects, of which 23 were males and 16 females. The samples were homogenised and extracted, and then cleaned-up by preparative gel permeation chromatography. The phenolic compounds were determined in silylated extracts. A total of 21 individual compounds were analysed in the extracts by gas chromatography-mass spectrometry (HRGC-LRMS) in the selected ion monitoring mode. The most commonly occurring compounds were 4-octylphenol diethoxylate, 4,4'-dihydroxybiphenyl, and 2,2',4,4'-tetrabromodiphenyl ether (BDE-47), but also some other alkylphenols, pentabromophenol, and 2,2',4,4',5-penta- and 2,2',4,4',5,5'-hexabromodiphenyl ether could be detected in 1-6 samples. The concentrations were ranging from trace amounts to 71 ng/g of lipid weight. The mean concentration of BDE-47 was 1.20 ng/g lipids, however, in 15 of the samples the concentration was below the detection limit. Compared to other European studies the average concentration of BDE-47 obtained in this study is at the lower end of the reported concentrations.
PubMed ID
14512116 View in PubMed
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[Characteristics of the aggregative state of the substrate in the reaction of 5-lipoxygenase oxidation of linoleic acid]

https://arctichealth.org/en/permalink/ahliterature10115
Source
Ukr Biokhim Zh. 2001 Mar-Apr;73(2):39-43
Publication Type
Article
Author
I A Butovich
O V Kharchenko
Iu N Paboka
M G Kazachkov
Author Affiliation
Institute of Bioorganic Chemistry and Petrochemistry of National Academy of Sciences of Ukraine, Kyiv.
Source
Ukr Biokhim Zh. 2001 Mar-Apr;73(2):39-43
Language
Russian
Publication Type
Article
Keywords
Arachidonate 5-Lipoxygenase - metabolism
Chromatography, Gel
Chromatography, Ion Exchange
English Abstract
Linoleic Acid - chemistry - metabolism
Micelles
Molecular Weight
Oxidation-Reduction
Abstract
5-lipoxygenase (EC 1.13.11.12) oxidizes polyunsaturated fatty acids by molecular oxygen. The enzyme acts in close contact with the cell membranes, which main components are ionic and non-ionic lipids. In order to investigate the kinetic parameters of 5-lipoxygenase reaction in vitro, extremely hydrophobic fatty acid substrate (linoleic acid) should be solubilized in the reaction mixture. We used Lubrol PX ("Sigma" Chem. Co), as a non-ionic detergent consisted of oligoethylene glycol and fatty alcohol. Linoleic acid and Lubrol PX formed mixed micelles thus solubilizing the fatty acid substrate in a buffer with appropriate pH. We have studied the sizes and shapes of mixed micelles Lubrol PX/linoleic acid (aggregates type 1) and Lubrol PX/linoleic acid/SDS (aggregates type 2; SDS was an effective activator of potato tuber 5-lipoxygenase) by means of gel-filtration and laser light scattering techniques. The parameters under investigation were molecular weights, Stocks radii and shapes of the mixed micelles. The average molecular weights and Stocks radii of the mixed micelles type 1 determined by mean of gel-filtration on Sephadex G-200 were 95,142 +/- 5184 Da and 3.45 +/- 0.11 nm, respectively. The same parameters for the mixed micelles type 2 were 73,694 +/- 893 Da and 3.02 +/- 0.02 nm, respectively. The strong similarity in physicochemical parameters for both types of mixed micelles indicated that SDS did not influence the size and shape of mixed micelles of Lubrol PX and linoleic acid. The activatory action of SDS on potato tuber lipoxygenase may be a result of electrostatic effect or direct participation of SDS in enzymatic catalysis. The laser light scattering technique allowed to determine two main fraction of particles in type 1 system with hydrodynamic diameters 2.6 and 5.7 nm and relative contribution to light scattering 13 and 87%, respectively. The particles with d = 5.7 nm were interpreted as the mixed micelles. The particles with d = 2.6 nm were interpreted as isolated molecules of Lubrol PX, linoleic acid and (or) their premicellar aggregates. The data obtained are to be used in creation of reliable physical and mathematical models of 5-lipoxygenase.
PubMed ID
11642042 View in PubMed
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Characterization of a new LCAT mutation causing familial LCAT deficiency (FLD) and the role of APOE as a modifier gene of the FLD phenotype.

https://arctichealth.org/en/permalink/ahliterature150387
Source
Atherosclerosis. 2009 Dec;207(2):452-7
Publication Type
Article
Date
Dec-2009
Author
Alexis Baass
Hanny Wassef
Michel Tremblay
Lise Bernier
Robert Dufour
Jean Davignon
Author Affiliation
Hyperlipidemia and Atherosclerosis Research Group, Clinical Research Institute of Montreal (IRCM), Montreal, QC, Canada. a.baass@umontreal.ca
Source
Atherosclerosis. 2009 Dec;207(2):452-7
Date
Dec-2009
Language
English
Publication Type
Article
Keywords
Adult
Aged
Apolipoprotein A-I - blood
Apolipoprotein E2 - blood - genetics
Apolipoproteins B - blood
Biological Markers - blood
Cholesterol, HDL - blood
Cholesterol, LDL - blood
Chromatography, Gel
DNA Mutational Analysis
Electrophoresis, Agar Gel
Frameshift Mutation
Genetic Predisposition to Disease
Heterozygote
Homozygote
Humans
Hyperlipoproteinemia Type III - blood - enzymology - genetics
Lecithin Acyltransferase Deficiency - blood - enzymology - genetics
Male
Middle Aged
Pedigree
Phenotype
Phosphatidylcholine-Sterol O-Acyltransferase - genetics
Quebec
Risk factors
Sequence Deletion
Triglycerides - blood
Young Adult
Abstract
Familial LCAT deficiency (FLD) is a disease characterized by a defect in the enzyme lecithin:cholesterol acyltransferase (LCAT) resulting in low HDL-C, premature corneal opacities, anemia as well as proteinuria and renal failure. We have identified the first French Canadian kindred with familial LCAT deficiency. Two brothers, presenting classical signs of FLD, were shown to be homozygous for a novel LCAT mutation. This c.102delG mutation occurs at the codon for His35 and causes a frameshift that stops transcription at codon 61 abolishing LCAT enzymatic activity both in vivo and in vitro. It has a dramatic effect on the lipoprotein profile, with an important reduction of HDL-C in both heterozygotes (22%) and homozygotes (88%) and a significant decrease in LDL-C in heterozygotes (35%) as well as homozygotes (58%). Furthermore, the lipoprotein profile differs markedly between the two affected brothers who had different APOE genotypes. We propose that APOE could be an important modifier gene explaining heterogeneity in lipoprotein profiles observed among FLD patients. Our results suggest that a LCAT-/- genotype associated with an APOE epsilon2 allele could be a novel mechanism leading to dysbetalipoproteinemia.
PubMed ID
19515369 View in PubMed
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Characterization of an intertidal zone metagenome oligoribonuclease and the role of the intermolecular disulfide bond for homodimer formation and nuclease activity.

https://arctichealth.org/en/permalink/ahliterature310051
Source
FEBS Open Bio. 2019 10; 9(10):1674-1688
Publication Type
Journal Article
Research Support, Non-U.S. Gov't
Date
10-2019
Author
Yvonne Piotrowski
Kristel Berg
David Paul Klebl
Ingar Leiros
Atle Noralf Larsen
Author Affiliation
Department of Chemistry, Faculty of Science and Technology, SIVA Innovation Centre, UiT - The Arctic University of Norway, Tromsø, Norway.
Source
FEBS Open Bio. 2019 10; 9(10):1674-1688
Date
10-2019
Language
English
Publication Type
Journal Article
Research Support, Non-U.S. Gov't
Keywords
Chromatography, Gel
Computational Biology
Crystallography, X-Ray
Disulfides - chemistry - metabolism
Exoribonucleases - chemistry - genetics - metabolism
Humans
Metagenome - genetics
Models, Molecular
Protein Conformation
Abstract
The gene encoding MG Orn has been identified from a metagenomic library created from the intertidal zone in Svalbard and encodes a protein of 184 amino acid residues. The mg orn gene has been cloned, recombinantly expressed in Escherichia coli, and purified to homogeneity. Biochemical characterization of the enzyme showed that it efficiently degrades short RNA oligonucleotide substrates of 2mer to 10mer of length and has an absolute requirement for divalent cations for optimal activity. The enzyme is more heat-labile than its counterpart from E. coli and exists as a homodimer in solution. The crystal structure of the enzyme has been determined to a resolution of 3.15 Å, indicating an important role of a disulfide bridge for the homodimer formation and as such for the function of MG Orn. Substitution of the Cys110 residue with either Gly or Ala hampered the dimer formation and severely affected the enzyme's ability to act on RNA. A conserved loop containing His128-Tyr129-Arg130 in the neighboring monomer is probably involved in efficient binding and processing of longer RNA substrates than diribonucleotides.
PubMed ID
31420950 View in PubMed
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53 records – page 1 of 6.