Ripka J E, Ryan J W, Valido F A, Chung A Y, Peterson C M, Urry R L
Department of Medicine, University of Miami School of Medicine, FL 33101.
Biochem Biophys Res Commun. 1993 Oct 29;196(2):503-8. doi: 10.1006/bbrc.1993.2278.
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.
为了帮助阐明体细胞血管紧张素转换酶（ACE）各种形式的分子量和表面电荷异质性的基础，我们研究了N-糖基化的差异。从人、豚鼠、大鼠和兔组织中纯化的ACE制剂在N-糖基化位点数量（每分子ACE有7-8个位点）和用于糖基化的寡糖结构类型（复合寡糖与高甘露糖寡糖含量）方面存在异质性。我们的研究结果与潜在N-糖基化位点的报告和氨基酸测序数据相结合，表明ACE的各种形式在糖基化程度、糖基化位点和连接的寡糖单元结构方面可能存在差异。
