| First Author | Kurkinen M | Year | 1987 |
| Journal | J Biol Chem | Volume | 262 |
| Issue | 18 | Pages | 8496-9 |
| PubMed ID | 3597383 | Mgi Jnum | J:15730 |
| Mgi Id | MGI:63845 | Doi | 10.1016/s0021-9258(18)47441-8 |
| Citation | Kurkinen M, et al. (1987) Extensive homology between the carboxyl-terminal peptides of mouse alpha 1(IV) and alpha 2(IV) collagen. J Biol Chem 262(18):8496-9 |
| abstractText | We have determined the complete primary structure for the carboxyl-terminal peptides of mouse alpha 1(IV) and alpha 2(IV) collagen; which have 229 and 227 amino acids, respectively. The amino acid sequences are 63% identical and conservatively substituted in 28 positions. A striking feature of these peptides is that the first half of each sequence is homologous with the second half, 37% in alpha 1(IV) and 36% in alpha 2(IV). These results suggest that the carboxyl-terminal peptides of type IV collagen are closely related in their structure and evolution. Presumably, they were first derived by internal duplication of a common ancestral DNA sequence which later, by gene duplication, gave rise to the two different but homologous carboxyl-terminal peptides of type IV collagen. |
