抄録
Surface activity of silk fibroin and four water-soluble proteins was estimated quantitatively using polarography. Maxima which occur on current-voltage curve of reducible substances like oxygen can be suppressed by the addition of surface-active substances. Surface activity of proteins was estimated by the extent of the suppression of the oxygen maximum.
At the interface mercury-water, the proteins were more surface-active in 0.01M-KCl (pH6) than in 0.01M-(CH3COOH+CH3COONa) (pH4) and also at 40°C than at 30°C. The extent of the suppression of the oxygen maximum in 0.01M-KCl at 40°C increased in the following order:
egg albumin> serum albumin> hemogrobin> gelatin> silk fibroin
