Purification and partial characterization of a ...
Description
Citation
| Title | Purification and partial characterization of a rainbow trout egg lectin |
| Author(s) | R. Bildfell, R. Markham, G. Johnson |
| Journal | Journal of Aquatic Animal Health |
| Date | 1992 |
| Volume | 4 |
| Issue | 2 |
| Start page | 97 |
| End page | 105 |
| Abstract | A lectin that agglutinates rabbit red blood cells (RBCs) and human type B RBCs was isolated from ova of rainbow trout Oncorhynchus mykiss . Partial purification of this hemagglutinating material was achieved by affinity chromatography of an H sub(2)O-dialyzed yolk homogenate on rhamnose-linked Sepharose. Polyacrylamide gel electrophoresis (SDS-PAGE) revealed two polypeptides with approximate molecular masses of 19 kilodaltons (kDa) and 30 kDa. Proteins with a molecular mass of less than 20 kDa were separated from other elements of the affinity-purified hemagglutinating material. These proteins were found to lack hemagglutinating activity. When a western blot with rabbit antilectin antiserum was performed against yolk extract, rainbow trout serum, or yolk from larvae, a 30-kDa polypeptide was detected within all three samples. If these lectins are the same molecule, the biological function of the rainbow trout egg lectin may include host defense or perhaps a basic, homeostatic mechanism such as glycoprotein transport. |
| ISSN | 0899-7659 |
Using APA 6th Edition citation style.
[Page generation failure. The bibliography processor requires a browser with Javascript enabled.]
Times viewed: 63
