Abstract
An avian leukosis group-specific antigen (gs-a) was isolated from Tween-ether treated avian myeloblastosis virus (AMV) by cellulose acetate electrophoresis. Antigen and protein moved as a single component on Sephadex G-100 column chromatography and on polyacrylamide gel electrophoresis at pH 4.3 and 8.5. Calibration with proteins of known molecular weight of the Sephadex G-100 column and the pH 8.5 gel [containing 0.1% sodium dodecyl sulfate (SDS)] allowed estimation of the molecular weight of the antigen as about 20,000, consistent with earlier studies using ultracentrifugation. The N-terminal amino acid was determined by digestion of the protein with leucine aminopeptidase and by reaction with 14C-labeled fluorodinitrobenzene (FDNB) and 35S-labeled phenylisothiocyanate (PITC). All results indicated that proline was an N-terminal group. Using 35S-PITC, it was shown that there was one N-terminal proline per mole of gs-a.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 32-41 |
| Number of pages | 10 |
| Journal | Virology |
| Volume | 38 |
| Issue number | 1 |
| DOIs | |
| State | Published - May 1969 |
Bibliographical note
Funding Information:1 Support was provided cer Society, Inc., Grant Atomic Energy Contract 2 This is publication Commission of Harvard