Amine Modification of Digested Peptide at C-Terminal End during Protein Digestion by Protease
-
- Ito Toshiyuki
- Department of Biochemistry, Faculty of Pharmaceutical Sciences, Josai University
-
- Sugita Yoshiaki
- Department of Human Nutrition and Clinical Dietetics, Faculty of Pharmaceutical Sciences, Josai University
-
- Takao Koichi
- Department of Human Nutrition and Clinical Dietetics, Faculty of Pharmaceutical Sciences, Josai University
-
- Ikeguchi Yoshihiko
- Department of Biochemistry, Faculty of Pharmaceutical Sciences, Josai University
-
- Shirahata Akira
- Department of Biochemistry, Faculty of Pharmaceutical Sciences, Josai University Department of Human Nutrition and Clinical Dietetics, Faculty of Pharmaceutical Sciences, Josai University
Search this article
Abstract
We recently reported that C-terminal polyamine modification occurs when proteins are digested with trypsin in the presence of polyamine [Biochem. Biophys. Res. Commun., 356, 159—162 (2007)]. In the present study, the characteristics of this C-terminal modification in the presence of protease and amine were investigated. When hemoglobin (HB) was digested with trypsin in the presence of N-(2-pyridyl)-1,4-diaminobutane (Py4), formation of the modified peptide was dependent on time and on HB or Py4 concentration. When synthetic peptide was treated with trypsin in the presence of Py4, ca. 0.1% of the peptide was modified with Py4. When HB or cytochrome C was treated with a range of serine proteases in the presence of various amines (Py4, N-(2-pyridyl)-1,3-diaminopropane, tranexamic acid, isonicotinic acid hydrazide and ampicillin), the modified peptide was detected in all cases tested, thus suggesting that amine modification widely accompanies digestion by proteases.
Journal
-
- Biological and Pharmaceutical Bulletin
-
Biological and Pharmaceutical Bulletin 30 (10), 1838-1843, 2007
The Pharmaceutical Society of Japan
- Tweet
Keywords
Details 詳細情報について
-
- CRID
- 1390282679601079168
-
- NII Article ID
- 110006436360
-
- NII Book ID
- AA10885497
-
- ISSN
- 13475215
- 09186158
-
- NDL BIB ID
- 8918913
-
- Text Lang
- en
-
- Data Source
-
- JaLC
- NDL
- Crossref
- CiNii Articles
-
- Abstract License Flag
- Disallowed