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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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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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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).
C W, Heizmann, U, Kagi
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GABAergic septohippocampal neurons contain parvalbumin
Brain Research, 1989Septal axons were visualized in the hippocampus by anterograde transport of Phaseolus vulgaris leucoagglutinin (PHAL) injected into the medial septal region, which contains large numbers of parvalbumin (PV)-immunoreactive somata. A proportion of the PHAL-labelled afferents in the hippocampus were shown to be immunoreactive for PV by immunostaining ...
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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.
C W, Heizmann +2 more
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Parvalbumin immunohistochemistry in denervated skeletal muscle
Neuropathology and Applied Neurobiology, 1994Parvalbumin is a calcium–binding protein which, in muscle, is mainly found in type 2B fibres, whereas type 1 fibres lack parvalbumin immunoreactivity. Previous studies have shown that this pattern is highly dependent upon motor neuron innervation and is modified in denervated, cross–reinnervated or chronic low–frequency stimulated muscles.
M, Olive, I, Ferrer
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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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[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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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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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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