2020
DOI: 10.1039/d0ra02712j
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Interaction mechanism of aloe-emodin with trypsin: molecular structure–affinity relationship and effect on biological activities

Abstract: The mechanism of interaction between AE and trypsin was studied firstly. The biological activity of both decreased after the interaction. These results provide a basis for the development and utilization of AE.

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Cited by 7 publications
(1 citation statement)
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“…They are so abundant that over 700 serine endopeptidases have been identified, accounting for a third of known peptidases [15]. They perform a variety of physiological functions such as digestion, immune response, blood clotting, fibrinolysis and reproduction [16]. For aquatic products, endogenous serine proteases may be present in the muscle tissue or digestive tract, such as myofibril-bound serine endopeptidase, sarcoplasmic serine proteinase, trypsin, etc.…”
Section: Introductionmentioning
confidence: 99%
“…They are so abundant that over 700 serine endopeptidases have been identified, accounting for a third of known peptidases [15]. They perform a variety of physiological functions such as digestion, immune response, blood clotting, fibrinolysis and reproduction [16]. For aquatic products, endogenous serine proteases may be present in the muscle tissue or digestive tract, such as myofibril-bound serine endopeptidase, sarcoplasmic serine proteinase, trypsin, etc.…”
Section: Introductionmentioning
confidence: 99%