Nondestructive amino acid analysis at the picomole level of proline-containing peptides using aminopeptidase M and prolidase: application to peptides containing tyrosine sulfate.
A micromethod for nondestructive amino acid analysis was developed. Peptides were digested with amino-peptidase M followed by prolidase. The whole procedure was performed in a microvial for the autosampler of the analyzer. The resulting method has a working range from 10 to 600 pmol, at least, of sample taken into work. The usefulness of the method was demonstrated by its ability to determine the sulfation of tyrosine preceding proline in chicken gastrin.
Johnsen
A H
AH
Department of Clinical Biochemistry, Rigshospitalet, University of Copenhagen, Denmark.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis*; D000626:Aminopeptidases; D000803:Angiotensin I / Q000737:chemistry; D000818:Animals; D018826:CD13 Antigens; D002645:Chickens; D004150:Dipeptidases; D005755:Gastrins / Q000737:chemistry; D006801:Humans; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D011392:Proline / Q000032:analysis; D014443:Tyrosine / Q000031:analogs & derivatives / Q000032:analysis
D000596:Amino Acids; D005755:Gastrins; D010455:Peptides; C005662:tyrosine O-sulfate; D014443:Tyrosine; D000803:Angiotensin I; D011392:Proline; D000626:Aminopeptidases; D018826:CD13 Antigens; D004150:Dipeptidases; C022449:proline dipeptidase