Polypeptide sequencing: Use of dipeptidylaminopeptidase I and gas chromatography/mass spectrometry
- Resource Type
- Authors
- R.M. Caprioli; D.E. Sutherland; W.E. Seifert
- Source
- Biochemical and Biophysical Research Communications. 55:67-75
- Subject
- Chromatography, Gas
Swine
Biophysics
Sequence (biology)
Mass spectrometry
Biochemistry
Mass Spectrometry
chemistry.chemical_compound
Hydrolysis
Methods
Animals
Insulin
Amino Acid Sequence
Molecular Biology
chemistry.chemical_classification
Chromatography
Dipeptide
Chemistry
Porcine insulin
Dipeptides
Cell Biology
Cathepsins
Amino acid
Evaluation Studies as Topic
Cattle
Gas chromatography
Gas chromatography–mass spectrometry
Peptides
Spleen
- Language
- ISSN
- 0006-291X
Summary A new method of sequencing polypeptides has been investigated in which the polypeptide is enzymatically hydrolyzed to dipeptides by the action of dipeptidylaminopeptidase I and the products identified by gas chromatography/mass spectrometry. The technique involves two hydrolyses, the original polypeptide and the des N-terminal amino acid polypeptide, providing overlapping dipeptide sequences. The technique is illustrated by the determination of the sequence of porcine insulin A chain, a polypeptide containing 21 amino acids. Methods and procedures using standard dipeptides are also described and the advantages and present limitations of the technique discussed.