Curtin University Homepage
  • Library
  • Help
    • Admin

    espace - Curtin’s institutional repository

    JavaScript is disabled for your browser. Some features of this site may not work without it.
    View Item 
    • espace Home
    • espace
    • Curtin Research Publications
    • View Item
    • espace Home
    • espace
    • Curtin Research Publications
    • View Item

    Practical Aspects of the Ligand-Binding and Enzymatic Properties of Human Serum Albumin

    Access Status
    Fulltext not available
    Authors
    Kragh-Hansen, U.
    Chuang, Victor
    Otagiri, M.
    Date
    2002
    Type
    Journal Article
    
    Metadata
    Show full item record
    Citation
    Kragh-Hansen, Ulrich and Chuang, Victor Tuan Giam and Otagiri, Masaki. 2002. Practical Aspects of the Ligand-Binding and Enzymatic Properties of Human Serum Albumin. Biological and Pharmaceutical Bulletin. 25 (6): pp. 695-704.
    Source Title
    Biological and Pharmaceutical Bulletin
    ISSN
    0918-6158
    School
    School of Pharmacy
    URI
    http://hdl.handle.net/20.500.11937/12581
    Collection
    • Curtin Research Publications
    Abstract

    Recent work with approaches like recombinant mutants and X-ray crystallography has given much new information about the ligand-binding properties of human serum albumin (HSA). The information increases the understanding of this unique transport and depot protein and could give a structural basis for the possible construction of therapeutic agents with altered HSA-binding properties. A tabulation of high-affinity binding sites for both endogenous and exogenous compounds has been made; it could be useful for the above-mentioned purpose, but it could also be of value when trying to predict potential drug interactions at the protein-binding level. Drug displacement is not always a complication to therapy; it can be used to increase the biological effect of a drug. However, due to rebinding at other sites, the increase in the free concentration of a displaced ligand can be less than expected.Drugs and drug metabolites can also interact covalently with HSA; thiol-containing drugs often bind to the single free cysteine residue of HSA, and glucuronidated drugs react irreversibly with other residues of the protein. Reversible binding of ligands is often stereospecific, and therefore immobilized HSA can be used to separate drug isomers. Albumin-containing dialysates are useful for extracorporeal removal of endogenous toxins and in the treatment of drug overdoses. HSA has different types of hydrolytic activities, which also can be stereospecific. The esterase-like property seems especially useful in converting prodrugs to active drugs in plasma.

    Related items

    Showing items related by title, author, creator and subject.

    • Long chain fatty acids alter the interactive binding of ligands to the two principal drug binding sites of human serum albumin
      Yamasaki, K.; Hyodo, S.; Taguchi, K.; Nishi, K.; Yamaotsu, N.; Hirono, S.; Chuang, Victor; Seo, H.; Maruyama, T.; Otagiri, M. (2017)
      A wide variety of drugs bind to human serum albumin (HSA) at its two principal sites, namely site I and site II. A number of reports indicate that drug binding to these two binding sites are not completely independent, ...
    • Molecular modelling of the interactions of complex carbohydrates with proteins
      Gandhi, Neha Sureshchandra (2011)
      Glycosaminoglycans (GAGs) are ubiquitous complex carbohydrate molecules present on the cell surfaces and in extracellular matrices (ECM) of vertebrate and invertebrate tissues. The interactions of sulphated GAGs such as ...
    • Albumin-drug interaction and its clinical implication
      Yamasaki, K.; Maruyama, T.; Chuang, Victor; Otagiri, M. (2013)
      Background: Human serum albumin acts as a reservoir and transport protein for endogenous (e.g. fatty acids or bilirubin) and exogenous compounds (e.g. drugs or nutrients) in the blood. The binding of a drug to albumin is ...
    Advanced search

    Browse

    Communities & CollectionsIssue DateAuthorTitleSubjectDocument TypeThis CollectionIssue DateAuthorTitleSubjectDocument Type

    My Account

    Admin

    Statistics

    Most Popular ItemsStatistics by CountryMost Popular Authors

    Follow Curtin

    • 
    • 
    • 
    • 
    • 

    CRICOS Provider Code: 00301JABN: 99 143 842 569TEQSA: PRV12158

    Copyright | Disclaimer | Privacy statement | Accessibility

    Curtin would like to pay respect to the Aboriginal and Torres Strait Islander members of our community by acknowledging the traditional owners of the land on which the Perth campus is located, the Whadjuk people of the Nyungar Nation; and on our Kalgoorlie campus, the Wongutha people of the North-Eastern Goldfields.