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Some Common Properties Between a Brain Protein that Is Modified by Posttranslational Arginylation and the Microtubule‐Associated STOP Protein
Author(s) -
Bongiovanni Guillermina,
Barra Héctor S.,
Hallak Marta E.
Publication year - 1994
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 - 10.1046/j.1471-4159.1994.63062295.x
Subject(s) - immunoprecipitation , protein a/g , protein g , hspa2 , retinoblastoma like protein 1 , tubulin , biology , vesicle associated membrane protein 8 , gel electrophoresis , ddb1 , microtubule , microbiology and biotechnology , biochemistry , polyacrylamide gel electrophoresis , chemistry , peptide sequence , antibody , dna binding protein , membrane protein , enzyme , fusion protein , gene , transcription factor , recombinant dna , membrane , immunology
Properties so far studied of the 125‐kDa 14 C‐arginylated protein from rat brain show remarkable similarities with those of the STOP (stable tubule only polypeptide) protein. On sodium dodecyl sulfate‐polyacrylamide gel electrophoresis the 125‐kDa 14 C‐arginylated protein moves to the same position as the STOP protein. The 125‐kDa 14 C‐arginylated protein was immunoprecipitated by the monoclonal Mab 296 antibody specific for neuronal STOP protein. The 125‐kDa 14 C‐arginylated protein was retained by a calmodulin column like STOP protein. As occurs with the STOP protein, the 125‐kDa 14 C‐arginylated protein is found in higher proportion in cold‐stable than in cold‐labile microtubules. However, the modified protein associates with microtubules in a lower proportion than the STOP protein. We conclude that the STOP protein incorporates arginine by a posttranslational reaction but that only a small fraction of the STOP protein shows acceptor capacity in vitro.