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Isolation and characterization of human reg protein produced in Saccharomyces cerevisiae
Author(s) -
Itoh Takako,
Tsuzuki Hiroshige,
Katoh Takaaki,
Teraoka Hiroshi,
Matsumoto Kohichi,
Yoshida Nobuo,
Terazono Kimio,
Watanabe Takuo,
Yonekura Hideto,
Yamamoto Hiroshi,
Okamoto Hiroshi
Publication year - 1990
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(90)80454-q
Subject(s) - saccharomyces cerevisiae , complementary dna , peptide sequence , amino acid , biochemistry , microbiology and biotechnology , recombinant dna , biology , signal peptide , pyroglutamic acid , gene
reg was originally identified a a gene expressed during the regeneration of insulin‐producing pancreatic β‐cells of the rat. We built an expression vector containing human reg cDNA to drive Saccharomyces cerevisiae to synthesize the reg protein, and purified it from the culture medium. The 144‐amino acid sequence of the recombinant protein was consistent with that deduced from the cDNA and genomic DNA sequence except that the signal sequence of 22 amino acids was eliminated, and the amino‐terminal residue of the protein was pyroglutamic acid. The secondary structure of the reg protein was predicted by determination of the intramolecular cystine linkage and of α‐helix and β‐sheet contents.