Results 171 to 180 of about 66,774 (189)

Binding of calcium by parvalbumin fragments

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1978
Parvalbumin fragments from carp pI 4.47 parvalbumin corresponding to its residues 1--75 and 76--108 bind Ca2+ with affinities corresponding to Kd 0.9 . 10(-4) M and Kd 3 . 10(-3) M, respectively.
J, Derancourt, J, Haiech, J F, Pechère
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Parvalbumin immunoreactivity in the rat retina

Neuroscience Letters, 1990
The distribution of the Ca2+ binding protein parvalbumin was studied in the rat retina with immunocytochemistry using a mouse monoclonal antibody. Specific parvalbumin immunoreactivity was identified within a subpopulation of ganglion cells and a subpopulation of amacrine cells.
P P, Sanna, K T, Keyser, E, Battenberg, F E, Bloom   +3 more
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Terbium replacement of calcium in parvalbumin

Journal of Molecular Biology, 1978
Abstract Carp muscle calcium binding parvalbumin, crystallized in 2.9 m -ammonium sulfate, can bind two Tb3+ ions, which displace the two Ca2+ ions normally present. The Ca2+ co-ordinated in the loop between the E and the F α-helices is displaced at low Tb3+ concentrations; whereas the Ca2+ at the CD site is replaced only at higher Tb3 ...
J, Sowadski, G, Cornick, R H, Kretsinger
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Parvalbumin – the major tropical fish allergen

Pediatric Allergy and Immunology, 2008
Fish allergy is common in countries where consumption is high. Asian nations are amongst the world’s largest consumers of fish but the allergen profiles of tropical fish are unknown. This study sought to evaluate the allergenicity of four commonly consumed tropical fish, the threadfin (Polynemus indicus), Indian anchovy (Stolephorus indicus), pomfret ...
Lim, D.L.-C., Neo, K.H., Yi, F.C., Chua, K.Y., Goh, D.L.-M., Shek, L.P.-C., Van, Bever H.P., Lee, B.W., Giam, Y.C.   +8 more
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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 Exists in Rat Endocrine Glands

Endocrinology, 1985
Simple and rapid purification procedures for parvalbumin, one of the Ca2+-binding proteins (extracted from rat skeletal muscle), were developed, and its antiserum was produced in rabbits to measure the parvalbumin content of various rat tissues by RIA. The heat treatment, ammonium sulfate fractionation, and trichloroacetic acid precipitation of soluble
T, Endo, K, Takazawa, T, Onaya
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PARVALBUMIN AFFECTS FISH ATHLETICISM

Journal of Experimental Biology, 2012
How quickly you escape a predator or whether you catch the next meal is one of the key factors that decides whether you contribute to the greatest experiment on earth: evolution. Athletic performance varies enormously from individual to individual, and muscle performance is probably the ...
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Shining light on parvalbumin interneuron plasticity

Trends in Pharmacological Sciences
Neuronal networks rely on a balance between the activity of excitatory and inhibitory neurons, each having distinct roles in regulating the flow of activity across brain circuits and signal processing. Recent work by Selten et al. uncovers how parvalbumin (PV)-expressing interneurons adjust their inhibitory inputs in response to activity changes ...
Hommersom, M.P., Hommersom, M.P., Schubert, D., Nadif Kasri, N.   +3 more
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Metal-specific structural changes in parvalbumin

Biochemical and Biophysical Research Communications, 2012
Parvalbumin is a small protein of EF-hand family whose main role is considered to be metal buffering. Recent evidences indicate that parvalbumin also fulfills more complicated functions, which may be determined by the diversity in structural changes in response to the binding of different metal cations.
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The Rat Parvalbumin Gene

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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