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Binding of calcium by parvalbumin fragments
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1978Parvalbumin 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 Isoforms in Zebrafish
Molecular Biology Reports, 2005By 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.
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The structure of the mouse parvalbumin gene
Mammalian Genome, 1992Parvalbumin (PV) is a calcium-binding protein of the EF-hand family, expressed mainly in fast contracting/relaxing muscles of vertebrates. We have isolated five overlapping genomic PV clones which overall span 28 kilobase pairs (kb) around the Pva locus on mouse Chromosome (Chr) 15. The positions of four introns were determined by DNA sequencing.
Schleef, M. +3 more
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The binding of calcium to muscular parvalbumins
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1972Abstract The binding of Ca 2+ to muscular parvalbumins from hake ( Merluccius merluccius ) and frog ( Rana esculenta ) has been measured at pH 6.7 using the 45 Ca-Chelex partition method. The results indicate that these proteins have two high affinity sites ( K d = 0.1·10 −6 –0.4·10 −6 M) and 3–6 sites with lower affinity ( K d = 2·10 −6 –9·10
G, Benzonana, J P, Capony, J F, Pechere
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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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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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Parvalbumin, Molecular and Functional Aspects
1990Parvalbumin 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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Terbium replacement of calcium in parvalbumin
Journal of Molecular Biology, 1978Abstract 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 as a metal-dependent antioxidant
Cell Calcium, 2014Parvalbumin (PA) is a Ca(2+)-binding protein of vertebrates massively expressed in tissues with high oxygen uptake and respectively elevated level of reactive oxygen species (ROS). To characterize antioxidant properties of PA, antioxidant capacity (AOC) of intact rat α-PA has been explored.
Sergei E, Permyakov +3 more
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Interaction of cupric ion with parvalbumin
Biophysical Chemistry, 1992Cod 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 +5 more
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Parvalbumin in rat superior colliculus
Neuroscience Letters, 1990Parvalbumin-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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