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The Amino Acid Sequence of the Tryptophan‐Containing Subunit (α‐Subunit) of Bovine Brain S‐100 Protein
Author(s) -
Isobe Toshiaki,
Okuyama Tsuneo
Publication year - 1981
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.1471-4159.1981.tb00488.x
Subject(s) - tryptophan , protein subunit , interleukin 10 receptor, alpha subunit , peptide sequence , biochemistry , gamma aminobutyric acid receptor subunit alpha 1 , g alpha subunit , tryptophan synthase , calmodulin , gi alpha subunit , amino acid , gamma subunit , biology , chemistry , enzyme , gene
The tryptophan‐containing subunit (α‐subunit) of bovine brain S‐100 protein was purified from a S ‐aminoethyl derivative of S‐100a protein, and its amino acid sequence was determined. The α‐subunit contained 93 residues, including one tryptophan, and had a molecular weight of 10,400. The sequence shows an extensive homology (58% identity) to the sequence of another “tryptophan‐free” subunit (β‐subunit) found in both S‐100a and S‐100b protein, and has a calcium binding site characteristic of the “E‐F hand” proteins, such as calmodulin or troponin C. The tryptophan residue is located at position 90 which is presumably adjacent to the C‐terminal end of the α‐helix following the calcium binding loop, and thus appears likely to serve as a specific probe in structure‐function studies of S‐100a protein.