Premium
Peptide mapping of recombinant human parathyroid hormone by enzymatic digestion and subsequent fast‐atom bombardment mass spectrometry
Author(s) -
Nabuchi Yoshiaki,
Kuboniwa Hitoshi,
Takasu Hisashi,
Asoh Yoshinori,
Ushio Hidetoshi
Publication year - 1995
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.1290090402
Subject(s) - chemistry , deamidation , peptide , trypsin , protease , fast atom bombardment , recombinant dna , mass spectrometry , chromatography , biochemistry , digestion (alchemy) , enzyme , molecular mass , gene
Peptide maps of recombinant human parathyroid hormone (rhPTH) were determined by both trypsin and V‐8 protease digestion with subsequent fast‐atom bombardment mass spectrometry (FAB‐MS). Coverage of the sequence was 85% when using trypsin and 90% when using V‐8 protease. Five rhPTH variants that were recombinantly produced as models of Asn deamidated type degradation products were measured, and molecular weight differences between their respective deamidated peptide fragments were completely detected. In the V‐8 protease digests of some variants, characteristic peptide ions caused by the deamidation were observed and this greatly facilitated the assignment and recognition of the deamidated position. Our data suggest that FAB‐mapping of rhPTH via the protease digestion methods used, appears to have great potential for structural investigations of the peptide.