Inhibition of the endothelin-converting enzyme by pepsin digests of food proteins.
Inhibitory activities toward the endothelin-converting enzyme (ECE) were detected in pepsin digests of bonito pyrolic appendix and beef. After Sep-Pak C18 fractionation, this activity from bonito and beef was recovered in the 50% and 25% ethanol fractions, respectively. Activities were also recovered in the ultrafiltrate (< 5000 Da), and disappeared after a pronase treatment. Therefore, these inhibitory activities may have peptidic properties.
Okitsu
M
M
School of Food and Nutritional Sciences, University of Shizuoka, Japan.
Morita
A
A
Kakitani
M
M
Okada
M
M
Yokogoshi
H
H
D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000037:antagonists & inhibitors*; D002417:Cattle; D005591:Chemical Fractionation; D004044:Dietary Proteins / Q000378:metabolism*; D000072396:Endothelin-Converting Enzymes; D000431:Ethanol / Q000737:chemistry; D005511:Food Handling; D008460:Meat; D008666:Metalloendopeptidases / Q000037:antagonists & inhibitors*; D010434:Pepsin A / Q000378:metabolism*; D011402:Pronase / Q000378:metabolism; D014413:Tuna; D014462:Ultrafiltration
D004044:Dietary Proteins; D000431:Ethanol; D016282:Aspartic Acid Endopeptidases; D010434:Pepsin A; D008666:Metalloendopeptidases; D011402:Pronase; D000072396:Endothelin-Converting Enzymes