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出 处:《感光科学与光化学》1993年第4期342-348,共7页Photographic Science and Photochemistry
摘 要:运用改进的SDS-PAGE法,对明胶中的不同构象的组份随抽提次序的变化进行定量的测定和研究。工作结果表明:比α分子量小的肽链组份可以分离出5个峰,以α_(p1-5)表示,最小的α_(p5)组份的分子量约3万,α_(p5)组份含量在第3和第4道胶中消失。α_p组份的分子量,随抽提次序增多而不断增大。β组份含量随抽提次序增多时变化不大。(最后一道高温抽提除外)。α_1与α_2两个不同构象的比值α_1/α_2,随抽提次序增加略有升高,但不明显,基本上在1±0.1左右,这与胶原中α_1/α_2比值差别较大。β组份变化情况也与α类似。唯独γ构象组份含量随抽提次序增加而几乎呈线性增大。本文对分子量比γ大的组份(简称作>γ)也进行了定量的表征,表明>γ组份的分子量在40万到80万之间。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 αp1-5. The MW of αp5 is approximately more than 30000 which appeared in the 1st and 2nd extractions but disappeared in the 3rd and 4th ones. The MW of αp 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.
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