Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.15.1 (ACE)
 18,300 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Recent investigations suggest angiotensin converting enzyme (ACE) activity is generally decreased in normotensive pregnancy, but less is known about the level of activity of this enzyme in hypertensive pregnant subjects. The primary source of ACE is vascular endothelium and it can be measured in serum or plasma. In a preliminary investigation, we measured and compared diastolic blood pressure and serum ACE activity in 14 uncomplicated pregnant subjects during the third trimester, and in 16 subjects of similar gestation duration hospitalized with pregnancy-induced hypertension PIH. No patient had a positive history for, or evidence of, pulmonary or other metabolic disease. Compared with levels in normal pregnancy, serum ACE activity was found to be significantly elevated in PIH. In this study, this increase was not due to differences between the groups in maternal chronologic age or gestational duration. Further studies are necessary to determine if the increase in ACE activity precedes or follows development of clinically apparent PIH. If the former is the case, ACE activity might be a useful indicator of risk for PIH.
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PMID:Angiotensin converting enzyme activity in hypertensive pregnancy. 282 97

The aim of this work was to compare the antioxidant and angiotensin converting enzyme (ACE) inhibitory properties of Moringa oleifera seed protein isolate (ISO) and its enzymatic protein hydrolysates. ISO was subjected to enzymatic (alcalase, pepsin and trypsin) hydrolysis to obtain alcalase isolate, pepsin isolate and trypsin isolate hydrolysates (AIH, PIH, TIH). Amino acid composition was similar for the samples except that TIH had lower Sulphur-containing amino acids while PIH was lower in tryptophan. All the samples were tested for antioxidant properties through free radical scavenging abilities such as 2,2 diphenyl-1-picrylhydrazyl (DPPH) and hydroxyl radical scavenging assays as well as ferric reducing antioxidant power (FRAP) and metal ion chelation assays. The maximum percentage inhibition obtained for the samples from the different assays are: DPPH, 36% (PIH); FRAP, 0.04% (PIH); hydroxyl radical scavenging activity, 42.98% (ISO); and inhibition of metal ion chelation, 29.46% (AIH). AIH (79.3%) had the highest ACE-inhibitory activity followed by TIH (75.1%) while PIH (43.0%) had the least. Generally, the hydrolysis process produced hydrolysates with improved antioxidant and ACE-inhibitory properties when compared to the isolate. We conclude that enzymatic hydrolysis with alcalase, pepsin and trypsin may be used to produce M. oleifera seed protein hydrolysates with potential to be used as ingredients for the formulation of functional foods and nutraceuticals.
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PMID:Amino acid composition and antioxidant properties of Moringa oleifera seed protein isolate and enzymatic hydrolysates. 3038 28