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Isolation and characterization of human reg protein produced in Saccharomyces cerevisiae.
- Source :
-
FEBS letters [FEBS Lett] 1990 Oct 15; Vol. 272 (1-2), pp. 85-8. - Publication Year :
- 1990
-
Abstract
- reg was originally identified as a gene expressed during the regeneration of insulin-producing pancreatic beta-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 alpha-helix and beta-sheet contents.
- Subjects :
- Amino Acid Sequence
Calcium-Binding Proteins genetics
Calcium-Binding Proteins isolation & purification
Cystine
DNA genetics
Disulfides
Humans
Lithostathine
Molecular Sequence Data
Protein Conformation
Recombinant Proteins biosynthesis
Recombinant Proteins chemistry
Calcium-Binding Proteins biosynthesis
Islets of Langerhans physiology
Nerve Tissue Proteins
Regeneration
Saccharomyces cerevisiae metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0014-5793
- Volume :
- 272
- Issue :
- 1-2
- Database :
- MEDLINE
- Journal :
- FEBS letters
- Publication Type :
- Academic Journal
- Accession number :
- 2226837
- Full Text :
- https://doi.org/10.1016/0014-5793(90)80454-q