Angiotensin I converting enzyme from human plasma

Jj, Lanzillo; Fanburg, B. L.

doi:10.1021/bi00644a015

Cited by 67 publications

(24 citation statements)

References 17 publications

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“…In the present study, the activity of ACE was reestablished to 88% of normal activity in the presence of Nethylmaleimide, which quenches the sulphydryl group of captopril by alkylation (Lanzillo et al, 1985). The role of zinc in ACE activity was also confirmed in the present study.…”

Section: Discussionsupporting

confidence: 83%

“…Affinity resins for ACE isolation have been used previously and partial purification of ACE has been achieved with several types of ligands. Multi-step protocols have been replaced progressively by simpler and less laborious chromatography procedures using an affinity gel with the potent converting enzyme inhibitor lisinopril (Lanzillo et al, 1980(Lanzillo et al, , 1985. The agarose gel affinity chromatography with lisinopril as a ligand has been used by other laboratories too (El-Dorry et al, 1982;Bull et al, 1985;Hooper and Turner, 1987).…”

Section: Discussionmentioning

confidence: 99%

“…Macrophages and Leydig cells in the testis also express this isozyme. In contrast, the germinal isozyme is unique to the testis, which expresses both isoenzymes at a ratio of 4:1(germinal:somatic) (Lanzillo et al, 1985). Transcription of testis ACE begins in late pachytene spermatocytes (Langford et al, 1993) or after meiosis (Sibony et al, 1994).…”

Section: Introductionmentioning

confidence: 99%

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Characterization of angiotensin-converting enzyme in canine testis

Sabeur¹,

Vo²,

Ball³

2001

Reproduction

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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.

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Section: Discussionsupporting

confidence: 83%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Characterization of angiotensin-converting enzyme in canine testis

Sabeur¹,

Vo²,

Ball³

2001

Reproduction

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“…Although ACE exists primarily as a membrane-bound enzyme, a soluble form is present under normal conditions in blood plasma, amniotic fluid, seminal plasma and other body fluids (reviewed in [5,7]). The enzyme in plasma seems to be catalytically identical with, and immunologically very similar to, membrane-bound somatic ACE [8], except that it lacks the hydrophobic anchoring domain [9]. While studying the mode of membrane anchorage of pig kidney ACE, we observed that the enzyme could be solubilized from the membrane in a time-and temperature-dependent manner by a post-translational proteolytic cleavage [10].…”

Section: Introductionmentioning

confidence: 99%

Angiotensin-converting enzyme secretase is inhibited by zinc metalloprotease inhibitors and requires its substrate to be inserted in a lipid bilayer

Parvathy

Oppong

Karran

et al. 1997

Biochemical Journal

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Mammalian angiotensin-converting enzyme (ACE ; EC 3.4.15.1) is one of several proteins that exist in both membrane-bound and soluble forms as a result of a post-translational proteolytic processing event. For ACE we have previously identified a metalloprotease (secretase) responsible for this proteolytic cleavage. The effect of a range of structurally related zinc metalloprotease inhibitors on the activity of the secretase has been examined. Batimastat (BB94) was the most potent inhibitor of the secretase in pig kidney microvillar membranes, displaying an IC &! of 0.47 µM, whereas TAPI-2 was slightly less potent (IC &! 18 µM). Removal of the thienothiomethyl substituent adjacent to the hydroxamic acid moiety or the substitution of the P2h substituent decreased the inhibitory potency of batimastat towards the secretase. Several other non-hydroxamate-based collagenase inhibitors were without inhibitory effect on the secretase, indicating that ACE secretase is a novel zinc metalloprotease that is related to, but distinct from, the matrix metalloproteases. The full-length amphipathic form of ACE was labelled selectively

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“…Antiserum against human plasma ACE was prepared in rabbits as previously described (22). Monospecificity was established by Ouchterlony double diffusion and confirmed by enzyme-linked immunosorbent assay (23,24).…”

Section: Methodsmentioning

confidence: 99%