Pulmonary angiotensin-converting enzyme antienzyme antibody

Das, Manjusri; Soffer, Richard L.

doi:10.1021/bi00668a022

Cited by 73 publications

(30 citation statements)

References 32 publications

(32 reference statements)

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“…ACE of both normal lung and sarcoid lymph node appeared in the void volume on filtration through a Sephadex G-200 column, unlike the smaller serum enzymes which filtered similarly in the included volume prior to lactate dehydrogenase. Serum ACE appears to correspond to a purified particulate glycoprotein ACE from rabbit lung (24) and may be derived from the larger tissue form, perhaps biologically, since this transformation could not be achieved by purification in vitro of the rabbit enzyme (24). However, ACE in sarcoid lymph node appeared to be more readily inactivated by heat than ACE from normal lung or lymph node, indicating that it may differ from the normal enzyme.…”

Section: Discussionmentioning

confidence: 94%

Markedly elevated angiotensin converting enzyme in lymph nodes containing non-necrotizing granulomas in sarcoidosis.

Silverstein¹,

Friedland²,

Lyons³

et al. 1976

Proc. Natl. Acad. Sci. U.S.A.

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Sarcoidosis is a disease of unknown etiology that is characterized by the generalized formation of granulomas and is accompanied by elevation in the serum in less than half the patients of angiotensin converting enzyme, a dipeptidyl carboxypeptidase that catalyzes the conversion of the decapeptide, angiotensin I, to the pressor octapeptide, angiotensin II, and L-histidyl-L-leucine. Mean activity of angiotensin converting enzyme was elevated generally more than 10-fold in

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Section: Discussionmentioning

confidence: 94%

Markedly elevated angiotensin converting enzyme in lymph nodes containing non-necrotizing granulomas in sarcoidosis.

Silverstein¹,

Friedland²,

Lyons³

et al. 1976

Proc. Natl. Acad. Sci. U.S.A.

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“…The turnover number for angiotensin I is about 7 times smaller than that observed with pulmonary angiotensin I-converting enzyme (257 sec" 1 ). 20 For the hydrolysis of hog renin substrate by purified hog renin a turnover number of 4.7 sec" 1 has recently been published as a preliminary estimate. 21 The relative percentage rate of hydrolysis is the most relevant parameter for comparison of different substrates at low, physiological concentrations.…”

Section: Discussionmentioning

confidence: 99%

Substrate specificity of tonin from rat submaxillary gland.

Schiller¹,

Demassieux²,

Boucher³

1976

Circulation Research

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SUMMARY The substrate specificity of tonin from rat submaxillary gland was examined with a series of synthetic peptides encompassing the C-terminus of the decapeptide substrate angiotensin I. In contrast to angioteosin I-converting enzyme from plasma or lung, only angiotensin I, (des-Asp')-angiotensin I, and ( IN RECENT reports 1 -* the identification and partial purification of an angiotensin I-converting enzyme from rat submaxillary gland was described. The enzyme, for which the name tonin has been suggested, 2 has recently been purified to homogeneity. 3 The subsequent enzymatic characterization revealed major differences between tonin and the classic angiotensin I-converting enzyme found in plasma, lung, and other tissues. 4 Compared to angiotensin I-converting enzyme, tonin has a much lower molecular weight of only 28,700, a different pH optimum (pH 6.5-7.2), and no chloride requirement for enzymatic activity. The inhibitors of angiotensin I-converting enzyme, ethylenediaminetetraacetic acid (EDTA), dipyridyl, and the pentapeptide Pyr-LysTrp-Ala-Pro have no effect on tonin which, on the other hand, is strongly inhibited by a plasma component. In contrast to the classic converting enzyme, tonin is devoid of kininase II activity. Preliminary studies with the frequently used tripeptide substrates of angiotensin I-converting enzyme showed that these compounds are very poor substrates of tonin. However, it was found that tonin can form angiotensin II directly from renin tetradecapeptide substrate by cleavage of the Phe-His bond. On the basis of the suspected high specificity of the enzyme and the presence of a strong plasma protein inhibitor, it has been suggested that tonin may play an important role in the local generation of angiotensin II in tissue. 1 The purpose of this study was to further elucidate the substrate specificity of tonin by use of a series of synthetic polypeptides related to the C-terminus of angiotensin I. One of these peptides, (des-Asp^angiotensin I, is of particular interest as a substrate for possible conversion to (des-Asp 1 )-angiotensin II (angiotensin III) which recently has been

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“…In vitro experiments a) Inhibition of rabbit lung ACE: The ACE used was solubilized from the particulate fraction of the rabbit lung with Nonidet-P40 and fractionated with DEAE-cellulose (DE 52, Whatman) according to the method of Das and Soffer (10).…”

Section: Methodsmentioning

confidence: 99%