Results 161 to 170 of about 45,557 (210)
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Binding of nucleotides to parvalbumins
Biochemical and Biophysical Research Communications, 1982Abstract 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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Structure and Function of Parvalbumin
1989Parvalbumins were first isolated from muscles of lower vertebrates and their primary structures and biochemical properties have been investigated intensively (for review see 1). Later, parvalbumins were also detected in skeletal muscles of higher vertebrates, and the rabbit and rat parvalbumin have been sequenced (for reviews see 2–4).
Heizmann CW, Kagi U
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Conformational studies on muscular parvalbumins cooperative binding of calcium (II) to parvalbumins
Biochimie, 19791H NMR and ORD were used to characterize the respective variations of tertiary structure and secondary structure of parvalbumins with calcium content ((Pa(O), without calcium and PaCa2 calcium saturated) and temperature. It has been observed that the tertiary structure can be lost without significant variation of the helical content.
A, Cave, M, Pages, P, Morin, C M, Dobson
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[Ca-inhibited binding of melittin with parvalbumin. A new role for parvalbumins?].
Molekuliarnaia biologiia, 1989It was found that pike parvalbumins pI 4.2 and 5.0 bind amphiphilic peptide melittin extracted from bee venom in an extraordinary Ca-dependent manner: in apo-state the protein forms a tight equimolar complex with melittin (Ka = 10(6) M-1 at 18 degrees C); in Ca- (and Mg-) loaded state it does not take place.
E A, Permiakov +4 more
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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 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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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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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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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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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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