Mass balance strategy for protein sequencing. Application to a protein with an extended DNPNNP repeating motif

The value of the mass balance strategy is illustrated in the sequence determination of S. aureus V8 protease. Capillary electrophoresis, electrospray mass spectrometry, and high performance tandem mass spectrometry are used as well as proteolysis and Edman degradation. The carboxy terminus is found...

Full description

Saved in:
Bibliographic Details
Published inInternational journal of peptide and protein research Vol. 40; no. 6; p. 546
Main Authors Hua, S, Vestling, M M, Murphy, C M, Bryant, D K, Height, J J, Fenselau, C, Theibert, J, Collins, J H
Format Journal Article
LanguageEnglish
Published Denmark 01.12.1992
Subjects
Amino Acid Sequence
Chromatography, High Pressure Liquid
Cyanogen Bromide - chemistry
Dinitrophenols - analysis
Dinitrophenols - chemistry
Electrophoresis - methods
Mass Spectrometry
Molecular Sequence Data
Molecular Weight
Oligopeptides - analysis
Oligopeptides - chemistry
Peptide Fragments - analysis
Peptide Mapping
Proteins - chemistry
Repetitive Sequences, Nucleic Acid
Sequence Analysis - methods
Serine Endopeptidases - chemistry
Online AccessGet more information

Cover

More Information
Summary:The value of the mass balance strategy is illustrated in the sequence determination of S. aureus V8 protease. Capillary electrophoresis, electrospray mass spectrometry, and high performance tandem mass spectrometry are used as well as proteolysis and Edman degradation. The carboxy terminus is found to contain 17 irregularly repeating units of the triptych motifs NNP and DNP, which provide a challenge to any strategy involving mapping, sequencing, and overlapping of hydrolytic peptides.
ISSN:0367-8377
DOI:10.1111/j.1399-3011.1992.tb00439.x