| First Author | Qin H | Year | 1994 |
| Journal | Biochem Biophys Res Commun | Volume | 200 |
| Issue | 3 | Pages | 1277-82 |
| PubMed ID | 8185576 | Mgi Jnum | J:18074 |
| Mgi Id | MGI:66093 | Doi | 10.1006/bbrc.1994.1589 |
| Citation | Qin H, et al. (1994) Isolation and structure of cat superfast myosin light chain-2 cDNA and evidence for the identity of its human homologue. Biochem Biophys Res Commun 200(3):1277-82 |
| abstractText | A full-length cDNA clone coding for superfast myosin light chain-2 (MyLC2) was isolated from an expression cDNA library prepared from cat masseter muscle and was fully characterized. The deduced amino acid sequence shares 58% overall identity with limb fast MyLC2, whereas homologies of the latter among higher vertebrates show 90% identity, indicating that superfast MyLC2 has diverged considerably from limb fast MyLC2 during evolution. Superfast MyLC2 cDNA has 89% nucleotide homology and 93% amino acid homology with a published novel human MyLC2 (MYL5), suggesting that MYL5 is a human homologue of the cat superfast MyLC2. Hybridization of a superfast MyLC2 isoform-specific probe reveals that expression of superfast MyLC2 in cat is confined to jaw-closing muscles. In conclusion, the present paper describes for the first time the cloning of a superfast myosin light chain coding sequence. |
