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Parvalbumin in Cat Brain: Isolation, Characterization, and Localization
Author(s) -
Stichel Christine C.,
Kägi Urs,
Heizmann Claus W.
Publication year - 1986
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1986.tb02829.x
Subject(s) - parvalbumin , polyclonal antibodies , biology , cats , microbiology and biotechnology , biochemistry , chemistry , antibody , medicine , neuroscience , immunology
Because of the increasing evidence that Ca 2+ ‐binding proteins have important regulating functions in nerve cells and because of the indications that there are species differences in the structures of these proteins, parvalbumin was purified from cat brain and muscle. Brain and muscle parvalbumins were found to be indistinguishable from each other in their biochemical and im‐munological properties. However, cat parvalbumin differs from all other mammalian parvalbumins by its apparently lower M r on sodium dodecyl sulfate‐polyacryl‐amide gel electrophoresis of 10–11K (compared to rat parvalbumin, 12K), and a lower pI of 4.6 (rat parvalbumin, 4.9), in the tryptic peptide maps, and in the immu‐nological properties, indicating a distinct primary structure. With the purified parvalbumin as antigen, polyclonal antibodies were raised in rabbits and these were subsequently used for immunohistochemical localizations of parvalbumin in the cat brain. In the visual cortices of adult cats immunoreactive neurons were present throughout layers II and IV. In cerebellar cortex. Pur‐kinje, basket, and stellate cells were immunoreactive. Comparison with staining patterns obtained with anti‐serum against rat parvalbumin revealed some cross‐reactivity but confirmed the existence of species differences in the antigenic structure of rat and cat parvalbumin.