• Login
    View Item 
    •   Home
    • The Manchester Institute Cancer Research UK
    • All Paterson Institute for Cancer Research
    • View Item
    •   Home
    • The Manchester Institute Cancer Research UK
    • All Paterson Institute for Cancer Research
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of ChristieCommunitiesTitleAuthorsIssue DateSubmit DateSubjectsThis CollectionTitleAuthorsIssue DateSubmit DateSubjectsProfilesView

    My Account

    LoginRegister

    Local Links

    The Christie WebsiteChristie Library and Knowledge Service

    Statistics

    Display statistics

    Investigation of the interaction of alkyl sulphates with serum albumin using the thiocyanate radical ion (SCN)2.

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Authors
    Eadsforth, C
    Power, D
    Thomas, E
    Affiliation
    Paterson Laboratories, Christie Hospital and Holt Radium Institute, Manchester M20 9BX
    Issue Date
    1976-11
    
    Metadata
    Show full item record
    Abstract
    The reaction of the radical anion -(SCN)2-, produced during pulse radilysis of aqueous KCNS solutions, have been used to study the binding of a range of alkyl sulphates to bovine (BSA) and human (HSA) serum albumin. At neutral pH, -(SCN)2- reacts chiefly with trytophan residues. Approximately ten high-affinity binding sites are detectable for compounds of chain length greater than C7. The results are interpreted in terms of a model in which one hydrophobic region in the protein, containing the tryptophan residues, can accommodate the ten ligand molecules. Electrostatic interactions with positively-charged groups surrounding the hydrophobic area are also involved in binding.
    Citation
    Investigation of the interaction of alkyl sulphates with serum albumin using the thiocyanate radical ion (SCN)2. 1976, 30 (5):449-57 Int J Radiat Biol Relat Stud Phys Chem Med
    Journal
    International Journal of Radiation Biology and Related Studies in Physics, Chemistry, and Medicine
    URI
    http://hdl.handle.net/10541/190836
    DOI
    10.1080/09553007614551261
    PubMed ID
    1087285
    Type
    Article
    Language
    en
    ISSN
    0020-7616
    ae974a485f413a2113503eed53cd6c53
    10.1080/09553007614551261
    Scopus Count
    Collections
    All Paterson Institute for Cancer Research

    entitlement

    Related articles

    • Interactions of alkyl sulphates with bovine-serum albumin studied using eaq--as a probe.
    • Authors: Eadsforth CV, Power DM, Thomas EW, Davies JV
    • Issue date: 1977 Mar
    • Oxidation reactions of a bovine serum albumin-bilirubin complex. A pulse radiolysis study.
    • Authors: Adhikari S, Gopinathan C
    • Issue date: 1996 Jan
    • Pulse radiolysis of aqueous thiocyanate solution.
    • Authors: Milosavljevic BH, Laverne JA
    • Issue date: 2005 Jan 13
    • Interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants: spectroscopy and modelling.
    • Authors: Gelamo EL, Silva CH, Imasato H, Tabak M
    • Issue date: 2002 Jan 31
    • Chain length dependency of fatty acid and carbamate binding to serum albumin.
    • Authors: Brown NA, Wilson AG, Bridges JW
    • Issue date: 1982 Dec 15
    DSpace software (copyright © 2002 - 2025)  DuraSpace
    Quick Guide | Contact Us
    Open Repository is a service operated by 
    Atmire NV
     

    Export search results

    The export option will allow you to export the current search results of the entered query to a file. Different formats are available for download. To export the items, click on the button corresponding with the preferred download format.

    By default, clicking on the export buttons will result in a download of the allowed maximum amount of items.

    To select a subset of the search results, click "Selective Export" button and make a selection of the items you want to export. The amount of items that can be exported at once is similarly restricted as the full export.

    After making a selection, click one of the export format buttons. The amount of items that will be exported is indicated in the bubble next to export format.