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  • 1
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 6 (1977), S. 559-570 
    ISSN: 0091-7419
    Keywords: rhodopsin ; rod cell membrane ; limited proteolysis ; phosphorylation site ; amino-terminal ; carboxy-terminal ; carbohydrate attachment ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The amino terminus of bovine rhodopsin is blocked and has the sequence x-Met-Asn(CHO)-Gly-Thr-Glu-Gly-Pro-Asn-Phe-Tyr-Val-Pro-Phe-Ser-Asn(CHO)-Lys-Thr-Gly-Val-Val-Arg, where CHO represents sites of carbohydrate attachment. The carboxyl-terminal sequence of rhodopsin is Val-Ser-Lys-Thr-Glu-Thr-Ser-Gln-Val-Ala-Pro-Ala. Upon short-term digestion of rod outer segment (ROS) membranes with thermolysin, opsin (∼ 35,000 daltons) is converted to a membrane-bound fragment O′ (∼ 30,500 daltons) and 2 peptides containing 12 amino acids are released from the carboxyl terminus of rhodopsin into the supernatant. Upon long-term digestion of ROS with thermolysin, opsin and O′ are replaced by the membrane-bound fragments F1 (∼25,000 daltons), and F2 (∼9,500 daltons). When 32P-ROS are digested, F2 carries the 32P. Both O′ and F1 contain the amino-terminal glycopeptide.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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