Purification and substrate specificity of bovine angiotensin-converting enzyme.

Rohrbach, Michael S.; B.Williams, Ella; Rolstad, Rebecca A.

doi:10.1016/s0021-9258(19)70123-9

Cited by 87 publications

(23 citation statements)

References 26 publications

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“…The location of an hydrophobic amino acid flanked by proline residues close to the C-terminal, such as, in the α s1 -casein fragment 23 FVVAPFP 29 , generated also a high score. This structure with proline at the C-terminal and antepenultimate positions and an aromatic residue as penultimate residue has been reported as important for ACE-inhibition . Besides, peptides displaying the amino acid motif proline-hydrophobic-proline have shown resistance to further proteolytic degradation .…”

Section: Resultsmentioning

confidence: 99%

“…This structure with proline at the C-terminal and antepenultimate positions and an aromatic residue as penultimate residue has been reported as important for ACE-inhibition. 36 Besides, peptides displaying the amino acid motif proline-hydrophobicproline have shown resistance to further proteolytic degradation. 37 In the bovine casein hydrolysate with L. lactis, the best ranked sequences displayed the dipeptide valine-phenylalanine FFVAPFPEVFGK 34 described by Karaki et al 38 Table 7 shows the identified peptides in these ovine and bovine casein hydrolysates that had previously been described as antihypertensive or ACE-inhibitors and their origin with regard to bacterial preparation.…”

Section: Journal Of Agricultural and Food Chemistrymentioning

confidence: 99%

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Casein Hydrolysates by Lactobacillus brevis and Lactococcus lactis Proteases: Peptide Profile Discriminates Strain-Dependent Enzyme Specificity

Bounouala

Roudj

Karam

et al. 2017

J. Agric. Food Chem.

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Casein from ovine and bovine milk were hydrolyzed with two extracellular protease preparations from Lactobacillus brevis and Lactococcus lactis. The hydrolysates were analyzed by HPLC-MS/MS for peptide identification. A strain-dependent peptide profile could be observed, regardless of the casein origin, and the specificity of these two proteases could be computationally ascribed. The cleavage pattern yielding phenylalanine, leucine, or tyrosine at C-terminal appeared both at L. lactis and Lb. brevis hydrolysates. However, the cleavage C-terminal to lysine was favored with Lb. brevis protease. The hydrolysates showed ACE-inhibitory activity with IC in the 16-70 μg/mL range. Ovine casein hydrolysates yielded greater ACE-inhibitory activity. Previously described antihypertensive and opioid peptides were found in these ovine and bovine casein hydrolysates and prediction of the antihypertensive activity of the sequences based on quantitative structure and activity relationship (QSAR) was performed. This approach might represent a useful classification tool regarding health-related properties prior to further purification.

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Section: Resultsmentioning

confidence: 99%

Section: Journal Of Agricultural and Food Chemistrymentioning

confidence: 99%

Casein Hydrolysates by Lactobacillus brevis and Lactococcus lactis Proteases: Peptide Profile Discriminates Strain-Dependent Enzyme Specificity

Bounouala

Roudj

Karam

et al. 2017

J. Agric. Food Chem.

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“…If rapid equilibrium assumptions are applied to Scheme II, values for a, ß, and KA can be obtained from the variations of An, and kcat with [CL], as described by Segel (1975) and modified by Rohrbach et al (1981). Km°/AKm and Lmax0/ AKmax are plotted against 1 / [CL], where Am°a nd Fmax°a re 3 The possibility that the "zero" chloride velocities are due to contaminating anions has been considered.…”

Section: Resultsmentioning

confidence: 99%

“…of the decapeptide angiotensin I to the potent vasoconstricting octapeptide angiotensin II and the inactivation of the vasodilating nonapeptide bradykinin (Soffer, 1976;Erdos, 1976;Peach, 1977). Studies with synthetic substrates have revealed that ACE can act on an extremely wide range of oligopeptides, its principal requirements being a free COOH terminus and a primary amide at the scissile bond (Elisseeva et al, 1971;Stevens et al, 1972;Cheung et al, 1980;Rohrbach et al, 1981).2 Thus, while angiotensin I and bradykinin are its only well-documented physiological substrates, the enzyme could potentially hydrolyze many peptides in vivo. The existence of such additional substrates, and of further functions for ACE beyond control of blood pressure, is suggested by the presence of the enzyme in a large number of tissues.…”

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confidence: 99%

Anion activation of angiotensin converting enzyme: dependence on nature of substrate

Shapiro¹,

Holmquist²,

Riordan³

1983

Biochemistry

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Anion activation of pulmonary angiotensin converting enzyme has been examined by using 23 furanacryloyl- and 3 benzoyl-tripeptides as substrates. Chloride stimulates hydrolysis of all substrates at least 24-fold. However, the kinetic mechanism, the amount of chloride required, and the effect of pH on activation, plus the relative activating potencies of various anions, are all strongly dependent on the substrate employed. Three substrate classes have been identified. Class I substrates appear to be hydrolyzed at pH 7.5 by an ordered bireactant mechanism in which anion must bind before substrate. The apparent activation constant (KA') for Cl- ranges from 75 to 150 mM at pH 7.5, doubles at pH 9.0, and decreases to about 3 mM at pH 6.0. Class II substrates, in contrast, are hydrolyzed by a nonessential activator mechanism. The kinetically determined KA' for Cl- at pH 7.5 ranges from 2.9 to 5.0 mM and changes only slightly with pH. Class III substrates are also hydrolyzed by a nonessential kinetic mechanism but one different from that followed by class II peptides. KA' values for Cl- at pH 7.5 measured with class III substrates are 18-30 mM. Class II substrates have Arg or Lys at the ultimate or penultimate position. The features distinguishing class I and III peptides are less clear, although all class III substrates identified have penultimate alanine residues. Possible explanations for this substrate dependence are offered.

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“…In another study, the ACE solubilized by trypsinization from the human lung was purified 2,660-fold [31]. Rohrbach et al [32] have purified the ACE 2,300-fold from a bovine lung. In this study, the purity and molecular weight of the ACE were checked by SDS-PAGE and two bands of 60 and 70 kDa were detected on the gel (Fig.…”

Section: Resultsmentioning

confidence: 99%

Investigation of inhibition effect of butanol and water extracts of Matricaria chamomilla L. on angiotensin‐converting enzyme purified from human plasma

Baş

Türkoğlu

Göz

2021

Biotech and App Biochem

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Angiotensin-converting enzyme (ACE) liable for the regulation of blood pressure was purified from human plasma by affinity chromatography. Impact of water and butanol extracts of Matricaria chamomilla L. on purity ACE was examined. ACE was purified using the affinity chromatography method. The enzyme activity was evaluated at 345 nm by a spectrophotometer. Extracts of M. chamomilla plant with butanol and water were prepared. Lisinopril was utilized as a specific inhibitor. ACE was purified 3,659-fold from human plasma and the specific activity was 1,350 EU/mg protein. The molecular weight and purity of ACE were found by SDS-PAGE and two bands of 60 and 70 kDa on the gel were detected. Water and butanol extracts of M. chamomilla demonstrated inhibitor impact on ACE activity. IC 50 constants for water and butanol extracts of M. chamomilla were computed to be 1.292 and 0.353 mg/mL, respectively. The type of inhibition for whole inhibitors was identified as noncompetitive. IC 50 and K i constants for lisinopril were calculated to be 0.781 and 0.662 nM, respectively. These results indicate that butanol and water extracts of M. chamomilla may have an ACE inhibitor potential.

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Purification and substrate specificity of bovine angiotensin-converting enzyme.

Cited by 87 publications

References 26 publications

Casein Hydrolysates by Lactobacillus brevis and Lactococcus lactis Proteases: Peptide Profile Discriminates Strain-Dependent Enzyme Specificity

Casein Hydrolysates by Lactobacillus brevis and Lactococcus lactis Proteases: Peptide Profile Discriminates Strain-Dependent Enzyme Specificity

Anion activation of angiotensin converting enzyme: dependence on nature of substrate

Investigation of inhibition effect of butanol and water extracts of Matricaria chamomilla L. on angiotensin‐converting enzyme purified from human plasma

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