scholarly journals Characterization of angiotensin-converting enzyme in canine testis

Reproduction ◽  
2001 ◽  
pp. 139-146 ◽  
Author(s):  
K Sabeur ◽  
AT Vo ◽  
BA Ball
Keyword(s):  
Enzyme Activity ◽  
Angiotensin Converting Enzyme ◽  
Affinity Chromatography ◽  
Ace Inhibitor ◽  
Specific Activity ◽  
Normal Activity ◽  
Seminiferous Tubules ◽  
Affinity Column ◽  
Converting Enzyme ◽  
Ace Activity

The aim of this study was to characterize angiotensin-converting enzyme (ACE) in canine testis. Detergent-extracted canine testes were sonicated in the presence of protease inhibitors and purified on an affinity column with the ACE inhibitor, lisinopril, as an affinity ligand for ACE. The fractions recovered were assessed for ACE enzyme activity via an enzyme kinetic microplate assay (at 330 nm) based on the hydrolysis of Fa-Phe-Gly-Gly (FAPGG) at pH 7.5 during an 8 min incubation. The specific activity of ACE in the starting testicular extracts was 3.53 +/- 0.99 mU mg(-1) protein with a 1588 times enrichment in ACE activity after lisinopril affinity chromatography (4239 +/- 2600 mU mg(-1) protein). The recovery efficiency of ACE after lisinopril affinity chromatography was 71.2%. The ACE activity in the detergent extracts and the purified fractions was inhibited significantly by 10 micromol captopril l(-1), a specific ACE inhibitor, and was restored to 88% of normal activity by the addition of the thiol-alkylating agent N-ethylmaleimide (0.5 mmol l(-1)) in the detergent extracts and the purified fractions incubated with captopril. The treatment of testicular extracts with 10 mmol EDTA l(-1) reduced the ACE activity significantly (5.40 +/- 1.26 versus 0.58 +/- 0.23 mU mg(-1)). The ACE activity was restored fully in the presence of zinc (5.28 +/- 0.70 mU mg(-1)). The anti-ACE antibody (raised against a 70 kDa protein from the periacrosomal plasma membrane of equine spermatozoa) recognized a 65-70 kDa protein in the detergent-extracted testes as well as in the affinity-purified fractions. This antibody also recognized a protein of similar molecular mass in ejaculated spermatozoa. ACE was localized in the periacrosomal area of the ejaculated spermatozoa and in spermatids in the seminiferous tubules. The results of this study demonstrate that ACE is present in canine testis and retains its enzyme activity after purification with lisinopril affinity chromatography. Activity of canine ACE is inhibited by captopril and EDTA and is restored in the presence of N-ethylmaleimide and zinc.

scholarly journals Carboxypeptidase activity common to viridans group streptococci cleaves angiotensin I to angiotensin II: an activity homologous to angiotensin-converting enzyme (ACE)

Microbiology ◽  
2011 ◽  
Vol 157 (7) ◽  
pp. 2143-2151 ◽  
Author(s):  
Derek W. S. Harty ◽  
Neil Hunter
Keyword(s):  
Amino Acid ◽  
Angiotensin Converting Enzyme ◽  
Specific Activity ◽  
Converting Enzyme ◽  
Gene Encoding ◽  
Human Fibrinogen ◽  
Amino Acid Homology ◽  
Bacterial Surface ◽  
Ace Activity ◽  
Viridans Group Streptococci

We have found that Streptococcus gordonii FSS2, an infective endocarditis (IE) isolate, expresses a dipeptidyl-carboxypeptidase with activity homologous to angiotensin-converting enzyme (ACE). The carboxypeptidase activity was purified to homogeneity as a complex/aggregate from a bacterial surface extract and was also active as a 165 kDa monomer. The specific activity for the carboxypeptidase activity was eightfold higher than that for recombinant human ACE. Selected ACE inhibitors, captopril, lisinopril and enalapril, did not inhibit the ACE activity. The carboxypeptidase also hydrolysed the Aα and Bβ-chains of human fibrinogen, which resulted in impaired fibrin formation by thrombin. The gene encoding ACE carboxypeptidase activity was sequenced and the inferred polypeptide product showed 99 % amino acid homology to SGO_0566, sgc, ‘challisin’ of S. gordonii CL1 Challis, and had no significant amino acid sequence homology to human ACE. Homologues of challisin ACE activity were commonly detected among the viridans group streptococci most often associated with IE.

scholarly journals The Chemical Compounds of Flacourtia rukam Leaves and Their Inhibition of Angiotensin-converting Enzyme (ACE) Activity

Molekul ◽  
2021 ◽  
Vol 16 (3) ◽  
pp. 219
Author(s):  
Muharni Muharni ◽  
Heni Yohandini ◽  
Elfita Elfita ◽  
Fitrya Fitrya ◽  
Ani Sarah ◽  
...  
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Antihypertensive Agent ◽  
Ace Inhibitor ◽  
Chemical Compounds ◽  
Antihypertensive Activity ◽  
Converting Enzyme ◽  
Isolation And Identification ◽  
Ace Activity ◽  
Reported Data ◽  
Ace Inhibitory

Flacourtia  rukam is a plant popular among people to treat hypertension, especially the Musi Banyuasin of south Sumatera, Indonesia. Isolation and identification of chemical compounds from F. rukam leaves and evaluation of their effects on antihypertensive activity have been conducted. Isolation of chemical compounds using chromatographic methods and identification using spectroscopic methods were compared with the reported data. The drug’s effects on antihypertension were determined using the  angiotensin converting enzyme (ACE) inhibitory method. Two compounds were first reported and isolated from the leaves of F. rukam and identified as apigenin (1) and lupeol (2). These compounds were demonstrated to be effective in treating antihypertension with IC50 656.51 ± 1.55 µg/mL for apigenin and 15.12 ± 0.72 µg/mL for lupeol. It can be concluded that  F. rukam leaves is a potential ACE inhibitor can be explored further as an effective antihypertensive agent.

scholarly journals The study of angiotensin converting enzyme isolation from crossbred rabbit lung and enzyme storage capacity in frozen conditions

Food Research ◽  
2020 ◽  
Vol 4 (4) ◽  
pp. 1082-1088
Author(s):  
V.M. Nguyen ◽  
T.T. Tran ◽  
H.N. Vo
Keyword(s):  
Enzyme Activity ◽  
Angiotensin Converting Enzyme ◽  
Ammonium Sulfate ◽  
G Protein ◽  
Specific Activity ◽  
Distilled Water ◽  
Converting Enzyme ◽  
Angiotensin Converting Enzyme Activity ◽  
Rabbit Lung ◽  
Extraction Solvent

The study was carried out to obtain angiotensin converting enzyme (ACE) with high specific activity and to evaluate the ability to maintain enzyme activity in extract products as well as in rabbit lungs using frozen condition. In the scope of the content, the study conducted an evaluation to select the appropriate extraction solvent of four solvents including acetone, ethanol, Tris-HCl and distilled water. Initially, the research results have helped determine distilled water as the suitable extraction solvent and the difference is not statistically significant compared to Tris-HCl solvent. Angiotensin converting enzyme extract that was obtained by distilled water solvent has a specific activity of 10.35 U/g protein. In addition, the study investigated the ability to maintain angiotensin converting enzyme activity in rabbit lung and crude enzyme product during frozen storage (-18±2°C). The results of the study showed that angiotensin converting enzyme activity could be maintained for 3 months in rabbit lungs and 4 months in the crude product. Besides, the study also used ammonium sulfate with different concentrations to conduct angiotensin converting enzyme collection from extract product. The results of this content help determine the use of saturated ammonium sulfate with concentrations of 50% to 60% for the highest efficiency. The precipitation process helped obtain ACE products with a purity of 4.22 times, the specific activity of 42.64 U/g protein and the recovery rate of ACE up to 29.37%.

Development of angiotensin-converting enzyme in fetal rat lungs

1979 ◽  
Vol 236 (1) ◽  
pp. R57-R60 ◽  
Author(s):  
K. B. Wallace ◽  
M. D. Bailie ◽  
J. B. Hook
Keyword(s):  
Enzyme Activity ◽  
Angiotensin Converting Enzyme ◽  
Renin Angiotensin System ◽  
Prenatal Development ◽  
Supernatant Fraction ◽  
Hydrolytic Cleavage ◽  
Converting Enzyme ◽  
Rat Lungs ◽  
Age Related ◽  
Ace Activity

Angiotensin-converting enzyme (ACE) catalyzes rapid hydrolytic cleavage of angiotensin I to form angiotensin II (AII). Inasmuch as converting enzyme activity is present at birth and increases postnatally to adult values it was of interest to determine the prenatal development of ACE. Converting enzyme activity was determined in the 20,000 x g supernatant fraction of lung homogenates using hippuryl-L-histidyl-L-leucine (HHL) as substrate. Hippuric acid liberated by the hydrolysis of HHL was quantified spectrophotometrically. ACE activity was first detectable at 18 days of gestation and increased fourfold prior to birth (21 days gestation). Pulmonary ACE activity of 1-day-old animals was twice that of fetuses at day 20 of gestation; however, this increase did not appear to result from ventilation alone. The Michaelis-Menten constant for fetal ACE (2.0 mM HHL) was not different from that calculated for ACE of adult rat lungs (2.6 mM). These data were interpreted to indicate that the age-related increase in ACE activity was due to greater ACE content as opposed to further activation of preexisting enzyme. This increase in fetal ACE activity may play an important role in preparing the renin-angiotensin system for postnatal function.

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