Results 181 to 190 of about 55,623 (223)
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Parvalbumin in Human Brain

Journal of Neurochemistry, 1985
Abstract: Parvalbumin was isolated from human cerebral cortex and biceps and triceps muscles by HPLC. The immunological properties of the human protein and the mobility in two‐dimensional polyacrylamide gels were similar to that of parvalbumin isolated from the muscles of rat, mouse, rabbit, and chicken.
M W, Berchtold   +2 more
openaire   +2 more sources

Detecting Fish Parvalbumin with Commercial Mouse Monoclonal Anti-frog Parvalbumin IgG

Journal of Agricultural and Food Chemistry, 2006
Parvalbumin is a calcium-binding muscle protein that is highly conserved across fish species and amphibians. It is the major cross-reactive allergen associated with both fish and frog allergy. We used two-dimensional electrophoretic and immunoblotting techniques to investigate the utility of a commercial monoclonal anti-frog parvalbumin IgG for ...
Lingyun, Chen   +4 more
openaire   +2 more sources

Parvalbumin as a Pleomorphic Protein

Current Protein & Peptide Science, 2017
Parvalbumin (PA) is a classical small, mostly cytosolic Ca2+-binding protein of the EF-hand superfamily expressed in vertebrates in a tissue- and cell-specific manner, serving as a magnesium/ calcium buffer. In the last decade novel data were published on structural peculiarities of PA, likely affecting its functionality.
Permyakov, Eugene   +2 more
openaire   +3 more sources

A novel method based on infrared spectroscopic inception-resnet networks for the detection of the major fish allergen parvalbumin.

Food Chemistry, 2020
We have developed a novel approach that involves inception-resnet network (IRN) modeling based on infrared spectroscopy (IR) for rapid and specific detection of the fish allergen parvalbumin.
Xiao-peng Zhang   +5 more
semanticscholar   +1 more source

Binding of nucleotides to parvalbumins

Biochemical and Biophysical Research Communications, 1982
Abstract Intrinsic fluorescence and equilibrium dialysis studies have shown that ATP and ADP bind to parvalbumin molecules with affinities allowing the complex formation at physiological concentrations of protein and nucleotides. The stoichiometry and association constants for the nucleotide binding to calcium-loaded, magnesium-loaded and metal free ...
E A, Permyakov   +4 more
openaire   +2 more sources

Parvalbumin in rat superior colliculus

Neuroscience Letters, 1990
Parvalbumin-like immunoreactivity (PA-LI) has been studied in sections of the superior colliculus (SC) of the rat and its distribution compared to the patterns of acetylcholinesterase (AChE) and cytochrome oxidase (CO) staining. In the intermediate layers it was found that PA-LI is spatially associated with AChE only in the medial part of the SC, but ...
R B, Illing, D M, Vogt, W B, Spatz
openaire   +2 more sources

Parvalbumin Isoforms in Zebrafish

Molecular Biology Reports, 2005
By using an analysis of existing genomic information it is concluded that in zebrafish nine genes encode parvalbumin (PV). These genes possess introns that differ in size and show nucleotide variability but they contain the same number of exons, and for each corresponding exon, the number of nucleotides therein are identical in all the paralogs.
openaire   +2 more sources

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