Abstract: In present study an attempt was made to correlate the change (content) of different conformation components in photo-gelatin and the extraction sequences used in gelatin manufacture with the aid of the improved SDS-PAGE method.The quantitaive determination of the conformation showed that the peptide chain with molecular weight less than that of α can be separated into 5 smell fraction (5 peaks) characterized as α_p1-5.The MW of α_p5 is approximately more than 30000 which appeared in the 1st and 2nd extractions but disappeared in the 3rd and 4th ones.The MW of α_p increases steadily with the increase of extraction times.The change of the β conformation components with the increase of the extraction times has been found to be of no serious extent (except the 5.th final extraction).The ratio of α₁ to α₂(α₁/α₂) increases only a bit with the increase of extraction times, basically, with flucturation 1±0.1.This ratio value is quite different from that contained in collagen.The change of β conformation is similar to a contrary to β, the content of γ conformation with the increase of extraction times has shown to be a grossy proportional correlation.Present study also quantitatively characterized the component with MW more than that of γ, their MW has been found to be ranked within 0.4-0,8 million.

Key words: contormation, SDS-PAGE method, photogelatin, extraction