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Evidence for the repetitive domain structure of pig calpastatin as demonstrated by cloning of complementary DNA
Author(s) -
Takano Emiko,
Maki Masatoshi,
Hatanaka Masakazu,
Mori Hirotaka,
Zenita Koichi,
Sakihama Toshiko,
Kannagi Reiji,
Marti Thomas,
Titani Koiti,
Murachi Takashi
Publication year - 1986
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(86)81017-1
Subject(s) - calpastatin , edman degradation , peptide sequence , complementary dna , nucleic acid sequence , microbiology and biotechnology , molecular cloning , biology , oligonucleotide , biochemistry , protein primary structure , amino acid , coding region , dna , sequence analysis , chemistry , gene , calpain , enzyme
A clone of complementary DNA (cDNA) coding for pig heart calpastatin was isolated using synthetic oligonucleotide probes. The amino acid sequence deduced from the nucleotide sequence revealed the occurrence of a repetitive sequence at the interval of 140 amino acids, substantiating the multidomain structure of calpastatin. A portion of the sequence of 251 amino acid residues predicted for pig heart calpastatin (107 kDa) was found to be identical with that of a peptide fragment derived from pig erythrocyte calpastatin (68 kDa) and sequenced by Edman degradation.