Results 181 to 190 of about 46,693 (216)
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Detecting Fish Parvalbumin with Commercial Mouse Monoclonal Anti-frog Parvalbumin IgG
Journal of Agricultural and Food Chemistry, 2006Parvalbumin 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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The structure and evolution of parvalbumins
Journal of Molecular Evolution, 19751. 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 +6 more
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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 +2 more
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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 +2 more
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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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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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Parvalbumin expression in the diaphragm of aged rats
Archives of Gerontology and Geriatrics, 1994Parvalbumin is a calcium-binding protein involved in the mechanism of Ca(++) exchange between the sarcoplasmic reticulum and the myofibrils. There is a direct correlation between the amount of parvalbumin and the velocity of contraction-relaxation of skeletal muscle fibers.
E A, Jeckel-Neto +3 more
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Muscular parvalbumins as homologous proteins
Comparative Biochemistry and Physiology, 1968Abstract Considerations of earlier and new data on the amino-acid composition of some small molecular weight components of the myogen of lower vertebrates suggests that they constitute a family of homologous proteins and that, in contrast to previous hypotheses, this situation might also apply to some components of the myogen of higher vertebrates.
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1988
Parvalbumin belongs to the family of high affinity Ca2+-binding proteins (Heizmann and Berchtold 1987). In mammals, parvalbumin is synthesized in high amounts in fast contracting/relaxing muscles in a development-dependent manner (Celio and Heizmann 1982; Berchtold and Means 1985). Parvalbumin is also expressed in nonmuscle tissues such as brain (Celio
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Parvalbumin belongs to the family of high affinity Ca2+-binding proteins (Heizmann and Berchtold 1987). In mammals, parvalbumin is synthesized in high amounts in fast contracting/relaxing muscles in a development-dependent manner (Celio and Heizmann 1982; Berchtold and Means 1985). Parvalbumin is also expressed in nonmuscle tissues such as brain (Celio
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Structural Organization of the Human Parvalbumin Gene
1989Several genes encoding Ca2+-binding proteins of the EF-hand type have been isolated from different species (for a recent review see1). Many structural features such as splice site positions with respect to the homologous amino acid sequences, are common among these genes. The original hypothesis put forward by Kretsinger2 that EF-hand type Ca2+-binding
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