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N-glycosylation of forms of angiotensin converting enzyme from four mammalian species.

Abstract：

:To help clarify bases for the molecular weight and surface charge heterogeneities of forms of somatic angiotensin converting enzyme (ACE), we examined for differences in N-glycosylation. ACE preparations purified from human, guinea pig, rat and rabbit tissues were found to be heterogeneous in terms of numbers of N-glycosylated sites (7-8 sites per molecule of ACE) and in types of structures of oligosaccharides used for glycosylation (complex versus high mannose oligosaccharide contents). Our findings, taken with reports of potential N-glycosylation sites and amino acid sequencing data, indicate that ACE forms can differ in terms of degrees of glycosylation, sites of glycosylation and structures of attached oligosaccharide units.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Ripka JE,Ryan JW,Valido FA,Chung AY,Peterson CM,Urry RL

doi

10.1006/bbrc.1993.2278

subject

Has Abstract

pub_date

1993-10-29 00:00:00

pages

503-8

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(83)72278-3

journal_volume

196

pub_type

杂志文章

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