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2000
Volume 12, Issue 3
  • ISSN: 0929-8665
  • E-ISSN: 1875-5305

Abstract

Copper was added to truncated, recombinant cystathionine β-synthase (CBS), and the enzyme activity was assessed by measuring the production of cystathionine. 10microM copper significantly decreased CBS activity by 50% while 25microM copper decreased CBS activity by 70%. This inhibition was negated when an analog of the N-terminus of human albumin, Asp-Ala-His-Lys (DAHK), a strong transition metal binding peptide, was added. The use of copper chelators could significantly reduce in vivo homocysteine levels.

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/content/journals/ppl/10.2174/0929866053587048
2005-04-01
2025-05-24
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  • Article Type:
    Review Article
Keyword(s): chelation; copper; cystathionine synthase; homocysteine; inhibition
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