Peptide mapping of recombinant human parathyroid hormone by enzymatic digestion and subsequent fast-atom bombardment mass spectrometry
| Autor: | Hisashi Takasu, Hitoshi Kuboniwa, Yoshinori Asoh, Yoshiaki Nabuchi, Hidetoshi Ushio |
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| Rok vydání: | 1995 |
| Předmět: |
medicine.medical_treatment
Molecular Sequence Data Peptide Spectrometry Mass Fast Atom Bombardment Mass spectrometry Peptide Mapping Analytical Chemistry law.invention law medicine Humans Trypsin Amino Acid Sequence Deamidation Gene Spectroscopy chemistry.chemical_classification Protease Chromatography Hydrolysis Organic Chemistry Serine Endopeptidases Fast atom bombardment Recombinant Proteins chemistry Biochemistry Parathyroid Hormone Recombinant DNA medicine.drug |
| Zdroj: | Rapid communications in mass spectrometry : RCM. 9(4) |
| ISSN: | 0951-4198 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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