نتایج جستجو برای: parvalbumin

تعداد نتایج: 2399  

2013
Harmen H. J. de Jongh Carlos López Robles Eefjan Timmerman Julie A. Nordlee Poi-Wah Lee Joseph L. Baumert Robert G. Hamilton Steve L. Taylor Stef J. Koppelman

Food-processing conditions may alter the allergenicity of food proteins by different means. In this study, the effect of the glycosylation as a result of thermal treatment on the digestibility and IgE-binding of codfish parvalbumin is investigated. Native and glycosylated parvalbumins were digested with pepsin at various conditions relevant for the gastrointestinal tract. Intact proteins and pe...

Journal: :iranian journal of allergy, asthma and immunology 0
mohsen mohamadi department of medical biotechnology, school of advanced technologies in medicine, tehran university of medical sciences, tehran, iran and immunology research center, iran university of medical sciences, tehran, iran reza falak immunology research center, iran university of medical sciences, tehran, iran and department of immunology, school of medicine, iran university of medical sciences, tehran, iran kobra mokhtarian immunology research center, iran university of medical sciences, tehran, iran mohammad reza khoramizadeh department of medical biotechnology, school of advanced technologies in medicine, tehran university of medical sciences, tehran, iran esmaeil sadroddiny department of medical biotechnology, school of advanced technologies in medicine, tehran university of medical sciences, tehran, iran gholam ali kardar department of medical biotechnology, school of advanced technologies in medicine, tehran university of medical sciences, tehran, iran and immunology, asthma and allergy research institute, tehran university of medical sciences, tehran,iran

our aim in this study was to identify and characterize allergic proteins in cooked wolf herring fish. we heated the crude extract alternatively at 50, 60, 70, 80, 90, and 100°c for one hour and results were compared by sodium dodecyl sulfate polyacrylamide gel electrophoresis (sds-page). also, proteins were immunoblotted with fish-sensitive patients’ sera. the major allergenic proteins were ide...

Journal: :The Journal of biological chemistry 1990
C M Hutnik J P MacManus D Banville A G Szabo

The calcium-induced conformational changes of the 108-amino acid residue proteins, cod III parvalbumin and oncomodulin, were compared using tryptophan as a sensitive spectroscopic probe. As native oncomodulin is devoid of tryptophan, site-specific mutagenesis was performed to create a mutant protein in which tryptophan was placed in the identical position (residue 102) as the single tryptophan ...

Journal: :The Journal of biological chemistry 1989
A L Swain R H Kretsinger E L Amma

Carp parvalbumin coordinates calcium through one carbonyl oxygen atom and the oxygen-containing side chains of 5 amino acid residues, or 4 residues and a water molecule, in a helix-loop-helix structural motif. Other calcium-binding proteins, including calmodulin and troponin C, also possess this unique calcium-binding design, which is designated EF-hand or calmodulin fold. Parvalbumin has two s...

Journal: :Brain research 1992
S R Lapper Y Smith A F Sadikot A Parent J P Bolam

The cortex projects heavily to the striatum and makes asymmetrical synaptic contact mainly with the spines of medium-sized densely spiny neurones. The possibility exists that corticostriatal terminals also make synaptic contact with classes of striatal interneurones. The primary objective of the present experiment was to determine whether parvalbumin-immunoreactive neurones, which represent a c...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1989
P A de Viragh K G Haglid M R Celio

The influence of chronic vitamin D3 application on the concentration of the four calcium-binding proteins parvalbumin, the 28-kDa calbindin-D, calmodulin, and S-100 was studied in various brain regions and in the kidney. Young rats were administered daily 20,000 international units of vitamin D3 per kg (body weight) over a period of 4 months. This chronic treatment resulted in a clinically mild...

Journal: :Circulation 2004
Fawzia Huq Djamel Lebeche Vivek Iyer Ronglih Liao Roger J Hajjar

BACKGROUND Impaired relaxation is a cardinal feature of senescent myocardial dysfunction. Recently, adenoviral gene transfer of parvalbumin, a small calcium-buffering protein found exclusively in skeletal muscle and neurons, has been shown to improve cardiomyocyte relaxation in disease models of diastolic dysfunction. The goal of this study was to investigate whether parvalbumin gene transfer c...

Journal: :Investigative ophthalmology & visual science 2006
Tae-Jin Kim Chang-Jin Jeon

PURPOSE Matching the neuron's morphology with its expression of a particular protein cannot be easily achieved by immunocytochemistry alone, as many proteins are expressed too weakly. In this study, a newly developed method was adopted to match mouse retinal ganglion cell (RGC) morphology with its expression of parvalbumin. METHODS Parvalbumin-containing ganglion cells were first identified b...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1999
P A Wahr D E Michele J M Metzger

Heart failure frequently involves diastolic dysfunction that is characterized by a prolonged relaxation. This prolonged relaxation is typically the result of a decreased rate of intracellular Ca(2+) sequestration. No effective treatment for this decreased Ca(2+) sequestration rate currently exists. As an approach to possibly correct diastolic dysfunction, we hypothesized that expression of the ...

Journal: :Molecular biology and evolution 1984
N Maeda D X Zhu W M Fitch

One major parvalbumin each was isolated from the skeletal muscle of two reptiles, a boa snake, Boa constrictor, and a map turtle, Graptemys geographica, while two parvalbumins were isolated from an amphibian, the salamander Amphiuma means. The amino acid sequences of all four parvalbumins were determined from the sequences of their tryptic peptides, which were ordered partially by homology to o...

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