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Inhibitory Effect of Copper on Cystathionine β-Synthase Activity: Protective Effect of an Analog of the Human Albumin N-Terminus

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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.

Keywords: chelation; copper; cystathionine synthase; homocysteine; inhibition

Document Type: Review Article


Affiliations: Department of Trauma Research and Trauma Services, Swedish Medical Center, 501 E. Hampden Avenue, Englewood, CO 80113, USA.

Publication date: 2005-04-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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