Identification of recombinant hirudin by-products by electrospray ionization mass spectrometry

被引：2

作者：

Lango, J ^{[1
]}

Salat, J ^{[1
]}

Barta, I ^{[1
]}

Ott, I ^{[1
]}

Ambrus, G ^{[1
]}

Simay, A ^{[1
]}

Roboz, J ^{[1
]}

Yu, Q ^{[1
]}

Ma, L ^{[1
]}

机构：

[1] INST DRUG RES LTD, BUDAPEST, HUNGARY

来源：

EUROPEAN MASS SPECTROMETRY | 1996年 / 2卷 / 06期

关键词：

recombinant hirudin; Saccharomyces; electrospray mass spectrometry;

D O I：

10.1255/ejms.46

中图分类号：

O64 [物理化学（理论化学）、化学物理学]; O56 [分子物理学、原子物理学];

学科分类号：

070203 ; 070304 ; 081704 ; 1406 ;

摘要：

Bioactive by-products with antithrombin activity were obtained during the production of recombinant hirudin, rHV1-Tyr63, by a biotechnological process based on a genetically-modified Saccharomyces strain, The by-products were separated using preparative high performance liquid chromatography, The molecular masses of five major and three minor analytes were determined by electrospray mass spectrometry to be in the 5060 to 6835 Da range, all within +/-0.9 Da of the calculated masses of the proposed structures, Interpreted in terms of the known amino acid sequence of recombinant hirudin (6964 Da), the major by-products corresponded to residues after scissions at the 46, 49, 61, 63 and 64 amino acid positions, while the minor by-products resulted after cleavages at the 51, 53 and 62 positions.

引用

页码：355 / 360

页数：6

共 14 条

[1] THE STRUCTURAL ELEMENTS OF HIRUDIN WHICH BIND TO THE FIBRINOGEN RECOGNITION SITE OF THROMBIN ARE EXCLUSIVELY LOCATED WITHIN ITS ACIDIC C-TERMINAL TAIL [J].