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Biochemistry, 1982
Neuronal parvalbumin has been isolated from rat brain and purified to homogeneity by high-performance liquid chromatography (HPLC) on reverse-phase supports. This procedure includes four consecutive chromatographic steps with an overall protein recovery of 74% and a 26 400-fold purification.
M W, Berchtold +2 more
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Neuronal parvalbumin has been isolated from rat brain and purified to homogeneity by high-performance liquid chromatography (HPLC) on reverse-phase supports. This procedure includes four consecutive chromatographic steps with an overall protein recovery of 74% and a 26 400-fold purification.
M W, Berchtold +2 more
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Coexistence of parvalbumin and glycine in the rat brainstem
Brain Research, 1990The coexistence of glycine- and PV-immunoreactivities was studied immunocytochemically in the nuclei of the superior olive, trapezoid body, cochlea and lateral lemniscus. All of the PV-immunoreactive neurons in the nuclei of the superior olive and trapezoid body were immunoreactive to glycine but not to GABA. In the dorsal cochlear nucleus, PV-positive
E, Aoki +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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Conformational studies on parvalbumins by circular dichroism
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1975Structural variations of two parvalbumins, Whiting III and Pike III, in various denaturing conditions, have been studied by circular dichroism. CD signals are depressed from 4 urea. For Pike III, acidic pH, sodium dodecyl sulfate or complete removal of Ca2+ show little effect in the far ultraviolet region but rather strong effects in the near ...
J, Closset, C, Gerday
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Shining light on parvalbumin interneuron plasticity
Trends in Pharmacological SciencesNeuronal 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. +3 more
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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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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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A comparison at the peptide level of muscular parvalbumins from several lower vertebrates
Comparative Biochemistry and Physiology, 1969J P Capony, J F Pechere
exaly