MALDI-MS FOR C-TERMINAL SEQUENCE DETERMINATION OF PEPTIDES AND PROTEINS DEGRADED BY CARBOXYPEPTIDASE-Y AND CARBOXYPEPTIDASE-P

被引：65

作者：

THIEDE, B

WITTMANNLIEBOLD, B

BIENERT, M

KRAUSE, E

机构：

[1] FORSCH INST MOLEK PHARMAKOL,D-10315 BERLIN,GERMANY

[2] MAX DELBRUCK ZENTRUM MOLEK MED,PROT CHEM ABT,D-13125 BERLIN,GERMANY

来源：

FEBS LETTERS | 1995年 / 357卷 / 01期

关键词：

MALDI-MS; C-TERMINAL SEQUENCING; CARBOXYPEPTIDASE;

D O I：

10.1016/0014-5793(94)01323-S

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) has been used for C-terminal amino acid sequence determination of peptides and proteins, The usefulness of MALDI-MS was demonstrated by analyzing peptide mixtures (C-terminal peptide ladder) which were generated by enzymatic digestion of substance P, glucagon, angiotensinogen, insulin B chain and myoglobin with the exopeptidases carboxypeptidase Y and P. The results clearly show that up to 11 amino acid residues can be determined in the pmol range by analyzing the molecular masses of the truncated peptides, For proteins it is possible to investigate enzymatic or chemical digests in the same manner.

引用

页码：65 / 69

页数：5

共 22 条

[1] STRATEGY FOR THE CHARACTERIZATION OF THE GLYCOPROTEIN ENDOGLUCANASE-I ISOLATED FROM TRICHODERMA-REESEI - COMBINATION OF PLASMA DESORPTION AND UV LASER DESORPTION TIME-OF-FLIGHT MASS-SPECTROMETRY [J].