Premium
Brain micro glutamic acid‐rich protein is the C‐terminal endpiece of the neurofilament 68‐kDa protein as determined by the primary sequence
Author(s) -
Isobe Toshiaki,
Okuyama Tsuneo
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80339-2
Subject(s) - neurofilament , glutamic acid , proteolysis , peptide sequence , biochemistry , amino acid , protease , protein primary structure , chemistry , protein sequencing , sequence (biology) , biology , microbiology and biotechnology , enzyme , gene , immunohistochemistry , immunology
The amino acid sequence of bovine brain micro glutamic acid‐rich protein was determined by analysis of tryptic and Trimeresurus flavoviridis protease peptides of the molecule. The protein comprised 82 amino acid residues and has an M r of 8992. The established sequence was highly homologous (90% identity) to the sequence of C‐terminal 82 residues of the neurofilament 68‐kDa protein from porcine spinal cord; there are differences of 8 residues which could be species‐specific amino acid substitutions. This indicates that the micro glutamic acid‐rich protein may arise by a restricted proteolysis of the neurofilament 68‐kDa protein, with the break occuring toward the C‐terminus.