Open AccessIsolation, partial amino acid sequence, and immunohistochemical localization of a brain-specific calcium-binding protein.
Author(s) -
Lois Winsky,
Hajime Nakata,
Brian M. Martin,
David M. Jacobowitz
Publication year - 1989
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.86.24.10139
Subject(s) - calretinin , polyclonal antibodies , isoelectric point , calcium binding protein , guinea pig , peptide sequence , biology , biochemistry , proteolytic enzymes , calcium , amino acid , binding protein , microbiology and biotechnology , chemistry , immunohistochemistry , antibody , enzyme , endocrinology , organic chemistry , gene , immunology
A calcium-binding protein (protein 10) having a molecular mass of 29 kDa and an isoelectric point of 5.3 was purified from guinea pig brain. The amino acid sequence of fragments from proteolytic digestion of protein 10 revealed an 86% sequence identity with a calcium-binding protein (calretinin) found in chicken retina. Polyclonal antibodies against protein 10 revealed a specific distribution of this protein within sensory neurons of auditory, visual, olfactory, nociceptive, and gustatory systems as well as other discrete neuronal circuits in rat and guinea pig brain, whereas no specific label was observed in any of several peripheral tissues examined.