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Inhibition of Angiotensin Ð Converting Enzyme by a Synthetic Peptide Fragment of Glyceraldehyde-3-phosphate Dehydrogenase

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Inhibition of Angiotensin Ð Converting Enzyme by a Synthetic Peptide Fragment of Glyceraldehyde-3-phosphate Dehydrogenase

Ewa Seweryn

a,

*, Artur Pe˛dyczak

b

and Teresa Banas´

a

a Wrocław Medical University, Department of Medical Biochemistry, Chałubin´skiego 10, 50Ð368 Wrocław. Poland. Fax: (+48) 0713285415. E-mail: ewo.seweryn@yahoo.com

b University of Wrocław, Department of Chemistry, Wrocław, Poland

* Author for correspondence and reprint requests

Z. Naturforsch.55 c,657Ð660 (2000); received January 10/April 11, 2000

Glyceraldehyde-3-phosphate Dehydrogenase, Angiotensin-Converting Enzyme Inhibitor, Synthetic Peptide

A novel inhibitor of angiotensinÐconverting enzyme (ACE) identical to a sequence part of human muscle glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was chemically syn- thesized. Amino acid sequence was as follows ProÐGluÐAsnÐIleÐLysÐTrpÐGlyÐ Asp. This peptide inhibited rabbit lung ACE with a Kivalue of 1.6µm. The inhibitor of ACE acts in a non-competitive manner. The amino acid sequence of the new inhibitor was com- pared of GAPDH from other sources.

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