Glycosylation of bovine pulmonary angiotensin-converting enzyme modulates its catalytic properties Научная публикация
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FEBS Letters
ISSN: 0014-5793 , E-ISSN: 1873-3468 |
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| Вых. Данные | Год: 1998, Том: 431, Номер: 2, Страницы: 255-258 Страниц : 4 DOI: 10.1016/S0014-5793(98)00767-4 | ||||
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Реферат:
To study the role of the oligosaccharide moiety in the catalytic properties of angiotensin-converting enzyme (ACE), we obtained asialo- and partially deglycosylated ACE by enzymatic treatment of two-domain somatic enzyme from bovine lung. Treated enzymes demonstrated appreciable, but different changes of catalytic properties in the reaction of the hydrolysis of N-substituted tripeptides, C-terminal analogs of angiotensin I and bradykinin among them, compared to those for native enzyme. Deglycosylation also altered the catalytic properties of a single N domain of bovine ACE. So, various patterns of glycosylation modulate substrate specificity of somatic ACE and may be the reason for functional heterogeneity of the enzyme.
Библиографическая ссылка:
Orth T.
, Voronov S.
, Binevski P.
, Saenger W.
, Kost O.
Glycosylation of bovine pulmonary angiotensin-converting enzyme modulates its catalytic properties
FEBS Letters. 1998. V.431. N2. P.255-258. DOI: 10.1016/S0014-5793(98)00767-4 Scopus OpenAlex
Glycosylation of bovine pulmonary angiotensin-converting enzyme modulates its catalytic properties
FEBS Letters. 1998. V.431. N2. P.255-258. DOI: 10.1016/S0014-5793(98)00767-4 Scopus OpenAlex
Идентификаторы БД:
| ≡ Scopus: | 2-s2.0-0032541090 |
| ≡ OpenAlex: | W2036433147 |
Цитирование в БД:
| ≡ Scopus | 17 |