Ca2+-Dependent Mobility Shift of Parvalbumin in One- and Two-Dimensional Gel-Electrophoresis View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1990

AUTHORS

H.-J. Gregersen , C. W. Heizmann , U. Kaegi , M. R. Celio

ABSTRACT

Under Ca2(+)-loaded conditions parvalbumin migrates in one- and two-dimensional gel-systems as a double-band or -spot whereas in Ca2(+)-free condition it appears as one band or spot. Parvalbumin (PV), a member of the family of calcium-binding proteins [1], was first described in 1934 [2] and occurs in fast-contracting muscles and in subpopulations of neurons in vertebrates and humans [3,4,5]. The physical characteristics of molecular weight (Mv 12 KD), isoelectric point (pI 4.9) and Ca2(+)-binding properties are established (PV binds 2 Ca2+ per molecule) [5,6]. Physiological roles discussed for PV range from trigger- to buffer-protein of intracellular Ca2(+)-ions [7]. In this paper we report an as yet not described mobility shift of PV in gel-electrophoresis after manipulation of the Ca2+ concentration, which may have implications for its physiological function. More... »

PAGES

89-91

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4684-5754-4_13

DOI

http://dx.doi.org/10.1007/978-1-4684-5754-4_13

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1031613967

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/2112827


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