Title : Oxidation of apolipoprotein(a) inhibits kringle-associated lysine binding: the loss of intrinsic protein fluorescence suggests a role for tryptophan residues in the lysine binding site.

Pub. Date : 1997 Nov

PMID : 9385634






4 Functional Relationships(s)
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Sentence
Compound Name
Protein Name
Organism
1 Oxidation of apolipoprotein(a) inhibits kringle-associated lysine binding: the loss of intrinsic protein fluorescence suggests a role for tryptophan residues in the lysine binding site. Lysine lipoprotein(a) Homo sapiens
2 Oxidation of apolipoprotein(a) inhibits kringle-associated lysine binding: the loss of intrinsic protein fluorescence suggests a role for tryptophan residues in the lysine binding site. Lysine lipoprotein(a) Homo sapiens
3 Lp(a) has been implicated in atherogenesis and thrombosis through the lysine binding site (LBS) affinity of its kringle domains. Lysine lipoprotein(a) Homo sapiens
4 AAPH treatment caused a time-dependent decrease in the number of functional Lp(a) or r-apo(a) molecules capable of binding to fibrin or lysine-Sepharose and in the intrinsic protein fluorescence of both Lp(a) and r-apo(a). Lysine lipoprotein(a) Homo sapiens