Hemorphins derived from hemoglobin have an inhibitory action on angiotensin converting enzyme activity.
The hemorphins are opioid active peptides, which are enzymatically released from the beta-chain of hemoglobin. In this paper we report an inhibitory effect of these peptides on angiotensin converting enzyme (ACE) activity, known to be involved in blood pressure regulation. The hemorphins were found to be quite stable in tissue extracts containing ACE, and their importance as naturally occurring ACE inhibitors is discussed.
Lantz
I
I
Uppsala University, Department of Pharmacology, Sweden.
Glämsta
E L
EL
Talbäck
L
L
Nyberg
F
F
D000595:Amino Acid Sequence; D000806:Angiotensin-Converting Enzyme Inhibitors / Q000494:pharmacology*; D001794:Blood Pressure / Q000502:physiology; D002851:Chromatography, High Pressure Liquid; D004492:Edetic Acid / Q000494:pharmacology; D006454:Hemoglobins / Q000302:isolation & purification / Q000378:metabolism / Q000494:pharmacology*; D006801:Humans; D008168:Lung / Q000201:enzymology; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification / Q000378:metabolism / Q000494:pharmacology*; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism
D000806:Angiotensin-Converting Enzyme Inhibitors; D006454:Hemoglobins; C070564:LVV-hemorphin 6; D010446:Peptide Fragments; C070563:hemorphin 6; C049857:hemorphin 4; D004492:Edetic Acid; D007703:Peptidyl-Dipeptidase A