| First Author | Smith MJ | Year | 1987 |
| Journal | J Mol Biol | Volume | 194 |
| Issue | 2 | Pages | 345-7 |
| PubMed ID | 3612811 | Mgi Jnum | J:24534 |
| Mgi Id | MGI:72272 | Doi | 10.1016/0022-2836(87)90381-0 |
| Citation | Smith MJ, et al. (1987) Isolation and identification of partial cDNA clones for endoplasmin, the major glycoprotein of mammalian endoplasmic reticulum. J Mol Biol 194(2):345-7 |
| abstractText | The amino acid sequences of peptides isolated from murine endoplasmin showed significant homology (approximately 50%) with sequences in the heat-shock proteins 90 and 83 of yeast and Drosophila, respectively, indicating that they are related proteins. Mixed oligonucleotide probes, deduced from the peptide sequences, were used to isolate cDNAs from a murine liver cDNA library. DNA sequencing confirmed the presence of a coding sequence for one of the endoplasmin peptides, formally establishing the authenticity of the cDNA. The identity of the murine and hamster endoplasmin sequences suggests a level of sequence conservation associated with proteins that perform a structural role in cells. |
