Quantitative Evaluation of the Contribution of Weak Lysine-binding Sites Present within Apolipoprotein(a) Kringle IV Types 6–8 to Lipoprotein(a) Assembly-Reference-Cited by-同舟云学术

Quantitative Evaluation of the Contribution of Weak Lysine-binding Sites Present within Apolipoprotein(a) Kringle IV Types 6–8 to Lipoprotein(a) Assembly

Published:2004-01 Issue:4 Volume:279 Page:2679-2688
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Becker Lev,Cook P.Michael,Wright Theodore G.,Koschinsky Marlys L.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference28 articles.

1. Identification of the cysteine residue in apolipoprotein(a) that mediates extracellular coupling with apolipoprotein B-100.

2. Cys4057 of apolipoprotein(a) is essential for lipoprotein(a) assembly.

3. cDNA sequence of human apolipoprotein(a) is homologous to plasminogen

4. The apolipoprotein(a) kringle IV repeats which differ from the major repeat kringle are present in variably-sized isoforms

5. Molecular definition of the extreme size polymorphism in apolipoprotein(a)

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