Abstract
Rat calpastatin cDNAs obtained by RT-PCR method were isolated and directly sequenced, this allowed the identification of two new variants both characterized by a 23 amino acids deletion at the end of the unique N-terminal domain L, increasing the number of functional isoforms. The deletion shows high homology to the amino acid sequence coded by exon 8 of human calpastatin gene and properly conserved splicing consensus sequences, suggesting exon skipping in domain L. Furthermore, three point mutations scattered along the coding region were found.
| Original language | English |
|---|---|
| Pages (from-to) | 721-725 |
| Number of pages | 5 |
| Journal | Biochemistry and Molecular Biology International |
| Volume | 30 |
| Issue number | 4 |
| Publication status | Published - 1993 |
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ASJC Scopus subject areas
- Biochemistry
- Genetics
- Molecular Biology
Cite this
Novel rat calpastatin mRNA variants. / Servadio, A.; Casari, G.
In: Biochemistry and Molecular Biology International, Vol. 30, No. 4, 1993, p. 721-725.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Novel rat calpastatin mRNA variants
AU - Servadio, A.
AU - Casari, G.
PY - 1993
Y1 - 1993
N2 - Rat calpastatin cDNAs obtained by RT-PCR method were isolated and directly sequenced, this allowed the identification of two new variants both characterized by a 23 amino acids deletion at the end of the unique N-terminal domain L, increasing the number of functional isoforms. The deletion shows high homology to the amino acid sequence coded by exon 8 of human calpastatin gene and properly conserved splicing consensus sequences, suggesting exon skipping in domain L. Furthermore, three point mutations scattered along the coding region were found.
AB - Rat calpastatin cDNAs obtained by RT-PCR method were isolated and directly sequenced, this allowed the identification of two new variants both characterized by a 23 amino acids deletion at the end of the unique N-terminal domain L, increasing the number of functional isoforms. The deletion shows high homology to the amino acid sequence coded by exon 8 of human calpastatin gene and properly conserved splicing consensus sequences, suggesting exon skipping in domain L. Furthermore, three point mutations scattered along the coding region were found.
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UR - http://www.scopus.com/inward/citedby.url?scp=0027250472&partnerID=8YFLogxK
M3 - Article
VL - 30
SP - 721
EP - 725
JO - Biochemistry and Molecular Biology International
JF - Biochemistry and Molecular Biology International
SN - 1039-9712
IS - 4
ER -