Investigation of angiotensin glycosylation by MALDI-TOF and ESI tandem mass spectrometry

被引：0

作者：

Park, SJ

Park, DH

Sul, S

Oh, SF

Park, OS

Chung, DS

Kim, HJ ^{[1
]}

Kim, MS

Lee, SW

机构：

[1] Seoul Natl Univ, Sch Chem, Seoul 151747, South Korea

[2] Korea Univ, Dept Chem, Seoul 136701, South Korea

[3] Korea Univ, Ctr Electro & Photo Respons Mol, Seoul 136701, South Korea

来源：

BULLETIN OF THE KOREAN CHEMICAL SOCIETY | 2004年 / 25卷 / 12期

关键词：

angiotensin; glycosylation; partial hydrolysis; MALDI-TOF MS; ESI MS/MS;

D O I：

暂无

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Angiotensin 1, a model decapeptide, was glycosylated and partially hydrolyzed with HCI (6 N, 80 degreesC, 4 h), aminopeptidase, and carboxypeptidase Y. A single peptide mass map obtained from truncated peptides in the partial acid hydrolysate of angiotensin and its glycosylation product mixture by matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry enabled sequencing of angiotensin by a combinatorial procedure. MALDI-TOF and electrospray ionization (ESI) tandem mass spectrometric results indicate that both the N-terminal amino group of aspartic acid and the guanidinium group of the second residue arginine are glycosylated.

引用

页码：1791 / 1800

页数：10

共 20 条

[1] Identification of in-gel digested proteins by complementary peptide mass fingerprinting and tandem mass spectrometry data obtained on an electrospray ionization quadrupole time-of-flight mass spectrometer [J].