These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: [Electrophoresis and electrofocusing of rhodopsin solubilized by triton X-100].
    Author: Shukoliukov SA, Chizhevich EP, Korchagin VP, Osipov VV, Tiurin VA.
    Journal: Biokhimiia; 1976 Jan; 41(1):75-80. PubMed ID: 1276263.
    Abstract:
    Detergent-rhodopsin micells (component I) were separated from other fast and slow migrating protein components under electrophoresis of triton X-100 solubilized bovine rod outer segments (ROS). Treatment of ROS by alum caused a complete disappearance of non-rhodopsin proteins and the appearance of slow migrating band (component II). Preliminary bleaching of dark extracts did not affect the migration rate of the component I. The addition of urea to solubilizing mixture caused the increase of component I content and the diffusity components I and II bands. The rate of electrophoretic migration and the content of components I and II sharply decreased together with the appearance of fast migrating pink-brown band after the addition of 2-mercaptoethanol. The extracts from alum-treated ROS were separated into 15-20 protein bands under acrylamide gel isoelectric focusing. Such protein heterogeneity probably depended on the ability of triton X-100 to form micells with different isoelectric points during the interaction with ampholines in the electric field. These micells, having different isoelectric points, are shown to contain one and the same protein--opsin.
    [Abstract] [Full Text] [Related] [New Search]