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Proteomic and Functional Characterization of Antimicrobial Peptides Derived from Fisheries Bycatch via Enzymatic Hydrolysis. [PDF]

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Galendi VBSB   +7 more
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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
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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
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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
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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
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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
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