| Autor: |
François-Gerard, C, Gerday, C, Beeley, J G |
| Zdroj: |
Biochemical Journal; February 1979, Vol. 177 Issue: 2 p679-685, 7p |
| Abstrakt: |
Ovomucoid from the egg white of turtle-dove (Streptopelia risoria) was purified and shown to be a glycoprotein of mol. wt. 29 400, with valine as N-terminal residue. It is an inhibitor of both trypsin and chymotrypsin, but has a lower affinity for trypsin than has hen ovomucoid. Turtle-dove ovomucoid contains antigenic activity cross-reacting with the blood-group-P1 antigen of human erythrocytes. Hen ovomucoid has no detectable blood group-P1 activity. The carbohydrate composition of turtle-dove ovomucoid differs from hen ovomucoid in having substantially higher galactose content. The possible relationship between carbohydrate composition and antigenic activity is discussed. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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