Rhesus monkey lipoprotein(a) binds to lysine Sepharose and U937 monocytoid cells less efficiently than human lipoprotein(a). Evidence for the dominant role of kringle 4(37).

@article{Scanu1993RhesusML,
  title={Rhesus monkey lipoprotein(a) binds to lysine Sepharose and U937 monocytoid cells less efficiently than human lipoprotein(a). Evidence for the dominant role of kringle 4(37).},
  author={AngeloM. Scanu and Lindsey A. Miles and Gunther M. Fless and Ditta Pfaffinger and James D. Eisenbart and Ekerete Jackson and Jane L. Hoover-Plow and Terence K. Brunck and Edward F Plow},
  journal={The Journal of clinical investigation},
  year={1993},
  volume={91 1},
  pages={
          283-91
        }
}
Rhesus lipoprotein(a) (Lp[a]) binds less efficiently than human Lp(a) to lysine-Sepharose and to cultured U937 cells. Studies using elastase-derived plasminogen fragments indicated that neither kringle 5 nor the protease domain of Lp(a) are required in these interactions pointing at an involvement of the K4 region. Comparative structural analyses of both the human and simian apo(a) K4 domain, together with molecular modeling studies, supported the conclusion that K4(37) plays a dominant role in… CONTINUE READING
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