Results 251 to 260 of about 71,563 (292)

Parvalbumin, Molecular and Functional Aspects

1990
Parvalbumin was the first calcium-binding protein to be crystallized (Kretsinger 1980). From these data, the EF-hand structural arrangement, common to many calcium-binding proteins, was deduced. Parvalbumin contains 3 EF-hands but only the two COOH-terminal domains bind calcium.
Heizmann CW, Röhrenbeck J, Kamphuis W
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Parvalbumin

1996
Abstract Parvalbumin (PV) is a soluble Ca2+-binding protein found at highest concentration in fast contracting/re/axing muscle fibers of vertebrates. In the muscle PV is believed to facilitate the transfer of Ca2+from the myofibrils to the sarcop/asmic reticulum.
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Interaction of cupric ion with parvalbumin

Biophysical Chemistry, 1992
Cod parvalbumin, a calcium-binding protein, possesses a specific Zn2+ (or Cu2+) binding site per molecule. This work employed fluorescence energy transfer techniques to measure the distance between the Zn2+ (Cu2+) site and the stronger Ca(2+)-binding site in parvalbumin.
E A, Permyakov, L P, Kalinichenko, V Y, Derezhkov, M, Antalik, D C, Meinholtz, L J, Berliner   +5 more
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Parvalbumin and calretinin in the avian thymus

Anatomy and Embryology, 1993
The avian thymic hormone, known to support the maturation of T-lymphocytes, is biochemically similar to parvalbumin. However, its exact cellular distribution in the thymus is unknown. We have therefore studied the occurrence of parvalbumin and other related calcium-binding proteins in this organ by immunohistochemistry during development and after ...
Király E, Celio MR
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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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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, Sue L, Hefle, Steve L, Taylor, Ines, Swoboda, Richard E, Goodman   +4 more
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Resurrecting prehistoric parvalbumins to explore the evolution of thermal compensation in extant Antarctic fish parvalbumins

Journal of Experimental Biology, 2012
SummaryParvalbumins (PVs) from Antarctic notothenioid fishes display a pattern of thermal adaptation that likely reflects evolutionary changes in protein conformational flexibility. We have used ancestral sequence reconstruction and homology modeling to identify two amino acid changes that could potentially account for the present thermal sensitivity ...
A Carl, Whittington, Timothy S, Moerland
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The structure and evolution of parvalbumins

Journal of Molecular Evolution, 1975
1. Parvalbumins were isolated from the white muscle of Cynoscion regalis, Leiostomus xanthurus, and Menticirrhus americanus of the Sciaenidae and Pomatomus saltatrix of the Pomatomidae. 2. Menticirrhus contains three isoparvalbumins. The other species contain two isoparvalbumins which are designated "fast" and "slow" in accord with their ...
B, Sullivan, J, Bonaventura, C, Bonaventura, L, Pennell, J, Elliott, R, Boyum, W, Lambie   +6 more
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Isolation of neuronal parvalbumin by high-performance liquid chromatography. Characterization and comparison with muscle parvalbumin

Biochemistry, 1982
Neuronal parvalbumin has been isolated from rat brain and purified to homogeneity by high-performance liquid chromatography (HPLC) on reverse-phase supports. This procedure includes four consecutive chromatographic steps with an overall protein recovery of 74% and a 26 400-fold purification.
M W, Berchtold, K J, Wilson, C W, Heizmann   +2 more
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Coexistence of parvalbumin and glycine in the rat brainstem

Brain Research, 1990
The coexistence of glycine- and PV-immunoreactivities was studied immunocytochemically in the nuclei of the superior olive, trapezoid body, cochlea and lateral lemniscus. All of the PV-immunoreactive neurons in the nuclei of the superior olive and trapezoid body were immunoreactive to glycine but not to GABA. In the dorsal cochlear nucleus, PV-positive
E, Aoki, R, Semba, A, Seto-Ohshima, C W, Heizmann, S, Kashiwamata   +4 more
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