| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10235563 | Process Biochemistry | 2012 | 8 Pages |
Abstract
⺠A novel prolyl endopeptidase (PEP) was purified to homogeneity from common carp. ⺠PEP prefers to hydrolyze MCA substrates containing proline residue. ⺠Peptide mass fingerprinting analysis testified the enzyme is PEP. ⺠PEP may function in fish collagen metabolism and protein decomposition.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Bioengineering
Authors
Meng-Xiang Wang, Chan Zhong, Qiu-Feng Cai, Guang-Ming Liu, Ling Zhang, Kenji Hara, Wen-Jin Su, Min-Jie Cao,