BIOPEP-UWM: Report
| ID | 1093 |
| Name | lysozyme precursor, silk moth (Bombyx mori) |
| sequence |
| Function: | |
| Number of residues | 120 |
| Chemical mass | 13806.4412 | Monoisotopic mass | 13797.6546 |
| Bibliographic data: | |
| Authors | |
| Abraham E.G., Nagaraju J., Salunke D., Gupta H.M., Datta R.K. | |
| Title | |
| Purification and partial characterization of an induced antibacterial protein in the silkworm, Bombyx mori. J. Invertebr. Pathol. 65:17-24. | |
| Year | Source |
| 1995 | Journal |
| Additional information: |
| Lysozyme type C and alpha-lactalbumin have similar primary sequence and structure. But they have different function. Lactalbumin promotes the conversion of galactosyltransferase to lactose synthase and is essential for milk production. Lysozyme catalyses the hydrolysis of bacterial cell wall polysaccharides; it has also been recruited for a digestive role in certain ruminants and colobine monkeys . Lactalbumins have the ability to bind calcium and such property is assigned to only a few lysozymes. |
| Database reference: | |||
| SWISS PROT entry name: LYC_BOMMO, accession number: P48816 |