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

Ewa Seweryn3*, A rtur Pędyczakb and Teresa Banaś3 a Wroclaw Medical University, Department of Medical Biochemistry, Chalubiriskiego 10, 50-368 Wroclaw. Poland. Fax: (+48) 0713285415. E-mail: [email protected] b University of Wroclaw, Department of Chemistry, Wroclaw, Poland * Author for correspondence and reprint requests Z. Naturforsch. 55c, 657-660 (2000); received January 10/April 11, 2000 Glyceraldehyde-3-phosphate Dehydrogenase, Angiotensin-Converting Enzyme Inhibitor, Synthetic Peptide A novel inhibitor of angiotensin converting 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 Pro Glu Asn lie Lys Trp Gly Asp. This peptide inhibited rabbit lung ACE with a acts in a non-competitive manner. The amino acid pared of GAPDH from other sources.