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    Biochim Biophys Acta. 1994 Oct 21;1227(1-2):41-5.

    A single point mutation (Trp72-->Arg) in human apo(a) kringle 4-37 associated with a lysine binding defect in Lp(a).

    Scanu AM, Pfaffinger D, Lee JC, Hinman J.

    Department of Medicine, University of Chicago, IL.

    Human lipoprotein(a) or Lp(a) binds, like plasminogen, to lysine Sepharose. However, contrary to plasminogen in which kringles 1 and 4 have been implicated, the binding site or sites on apo(a), the specific glycoprotein of Lp(a), have not been determined. For the first time we now report the occurrence of a human Lp(a) that has a mutant form of apo(a) where Arg has replaced Trp in position 72 of kringle 4-37 and is unable to bind to lysine Sepharose. This observation suggests that Trp72 of apo(a) kringle 4-37 may play a dominant role in lysine binding. Lysine binding has been associated with the thrombogenic potential of Lp(a). Thus, the Trp72-->Arg mutation may render Lp(a) 'benign' from the cardiovascular viewpoint.

    PMID: 7918682 [PubMed - indexed for MEDLINE]

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