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Calmodulin‐Binding Proteins Within the Slow Phase of Axonal Transport in the Rabbit Vagus Nerve Per Ekstrom and Martin Kanje
Author(s) -
Ekstrom Per,
Kanje Martin
Publication year - 1987
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.1471-4159.1987.tb03406.x
Subject(s) - nodose ganglion , calmodulin , vagus nerve , tubulin , ganglion , chemistry , methionine , polyacrylamide gel electrophoresis , microbiology and biotechnology , biochemistry , biology , anatomy , endocrinology , microtubule , enzyme , amino acid , stimulation
: Calmodulin‐binding proteins (CBPs) in the rabbit vagus nerve were studied by means of calmodulin‐Sepha‐rose affinity chromatography and polyacrylamide gel electrophoresis. The soluble fraction (10 5 g supernatant) of a nerve homogenate contained four CBPs with molecular weights of 44, 55, 91, and 93 kD, respectively. Slowly transported proteins were recovered in the vagus 3 days after injection of [ 35 S]methionine into the nodose ganglion. Four labelled CBPs with molecular weights of 44, 55, 69, and 83 kD, respectively were found. The nodose ganglion con tained two labelled CBPs, 44 and 55 kD. The 55‐kD CBP was identified as tubulin after immunoblotting. In separate experiments it was also shown that bovine brain tubulin bound to the calmodulin column.