Results 161 to 170 of about 46,693 (216)

Parvalbumin as a Pleomorphic Protein

Current Protein & Peptide Science, 2017
Parvalbumin (PA) is a classical small, mostly cytosolic Ca2+-binding protein of the EF-hand superfamily expressed in vertebrates in a tissue- and cell-specific manner, serving as a magnesium/ calcium buffer. In the last decade novel data were published on structural peculiarities of PA, likely affecting its functionality.
Permyakov, Eugene, Uversky, Vladimir, Permyakov, Sergei   +2 more
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Parvalbumin in Human Brain

Journal of Neurochemistry, 1985
Abstract: Parvalbumin was isolated from human cerebral cortex and biceps and triceps muscles by HPLC. The immunological properties of the human protein and the mobility in two‐dimensional polyacrylamide gels were similar to that of parvalbumin isolated from the muscles of rat, mouse, rabbit, and chicken.
M W, Berchtold, M R, Celio, C W, Heizmann   +2 more
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Binding of nucleotides to parvalbumins

Biochemical and Biophysical Research Communications, 1982
Abstract 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, L P, Kalinichenko, V V, Yarmolenko, E A, Burstein, C, Gerday   +4 more
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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.
Floyd E Bloom, F E Bloom
exaly   +3 more sources

Structure and Function of Parvalbumin

1989
Parvalbumins 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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[Ca-inhibited binding of melittin with parvalbumin. A new role for parvalbumins?].

Molekuliarnaia biologiia, 1989
It 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, V N, Medvedkin, G A, Koreneĭchuk, E G, Kostrzhevskaia, A G, Murzin   +4 more
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Conformational studies on muscular parvalbumins cooperative binding of calcium (II) to parvalbumins

Biochimie, 1979
1H 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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Parvalbumin and calretinin in the avian thymus

Anatomy and Embryology, 1993
The avian thymic hormone, known to support the maturation of T-lymphocytes, is biochemically similar to parvalbumin. However, its exact cellular distribution in the thymus is unknown. We have therefore studied the occurrence of parvalbumin and other related calcium-binding proteins in this organ by immunohistochemistry during development and after ...
Király E, Celio MR
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