Investigation of inhibition angiotensin-converting enzyme (ACE) activity and opioid activity of two hemorphins, LVV-hemorphin-5 and VV-hemorphin-5, isolated from a defined peptic hydrolysate of bovine hemoglobin

Neuropeptides
Q Zhao, J-M Piot

Abstract

Two peptides, LVV-hemorphin-5 and VV-hemorphin-5, were isolated from a defined peptic bovine hemoglobin hydrolysate by reversed-phase HPLC. These peptides were identified as 31-38 and 32-38 fragments of beta chain of bovine hemoglobin. Their inhibitory activity towards angiotensin-converting enzyme and opioid potency were determined. Since their amino acid sequences show close homology with spinorphin, which is found in human cerebrospinal fluid and in the bovine spinal cord, the possible physiological role in vivo of these peptides was discussed.

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Citations

Feb 26, 2004·Journal of Biochemical and Biophysical Methods·Anders FuglsangNiels C B Nyborg
Sep 11, 2008·Addiction Biology·Peter J Gebicke-Haerter, Felix Tretter
Mar 10, 2001·Biochemical and Biophysical Research Communications·J SzikraA Borsodi
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Jan 27, 2019·Drug Development Research·Petar TodorovJana Tchekalarova
Nov 12, 2019·Frontiers in Pharmacology·Amanat AliMohammed Akli Ayoub
Jan 1, 2021·International Journal of Molecular Sciences·Amanat AliRanjit Vijayan
Feb 20, 2020·Peptides·Fengmei WeiYuhong Jing
Apr 4, 2021·Pharmaceuticals·Mohammed Akli Ayoub, Ranjit Vijayan

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