Binding of a high reactive heparin to human apolipoprotein E: identification of two heparin-binding domains.

Abstract:

:Ligand-blotting and dot-blotting procedures were used to investigate the binding of [125I]-heparin to apolipoprotein E, its thrombin fragments E22 (residues 1-191) and E12 (residues 192-299), and to nine apolipoprotein E synthetic fragments. E22 and E12 bound [125I] heparin indicating multiple heparin-binding domains. Synthetic peptides of apoE corresponding to residues 129-169, 139-169, and 144-169, but not 148-169, bound [125I] heparin suggesting that residues 144-147 (Leu-Arg-Lys-Arg) in E22 are important for binding. Peptide 202-243 and 211-243 but not 219-243 bound [125I] heparin suggesting that residues 211-218 (Gly-Glu-Arg-Leu-Arg-Ala-Arg-Met) comprise a portion of the E12 heparin-binding domain.

authors

Cardin AD,Hirose N,Blankenship DT,Jackson RL,Harmony JA,Sparrow DA,Sparrow JT

doi

10.1016/s0006-291x(86)80489-2

subject

Has Abstract

pub_date

1986-01-29 00:00:00

pages

783-9

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(86)80489-2

journal_volume

134

pub_type

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