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Discover Supplement-Drug Interactions
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Last Updated: 3 years ago
supplement:
Chymotrypsin
Research Papers that Mention the Interaction
“Seven chymotryptic cleavage sites, Trp(60), Phe(61), Phe(75), Phe(84), Phe(113), Phe(118), and Tyr(122), located near or within the core alpha-crystallin domain, were shielded from the action of chymotrypsin in the presence of ATP.”
ATP and the core "alpha-Crystallin" domain of the small heat-shock protein alphaB-crystallin.“Our results indicated that the proteolytic susceptibilities of trypsin and chymotrypsin were altered in the presence of ATP.”
“In the presence of ATP, chymotrypsin rapidly cleaved the thymus myosin heavy chain at an additional site about 4000 daltons from the N-terminus.”
Effects of proteolysis on the adenosinetriphosphatase activities of thymus myosin.“The chymotryptic split appears to disrupt antagonistic interactions between cation and ATP binding domains, while the E1-E2 conformational transition of the unphosphorylated protein probably remains.”
“The presence of ATP restricts both trypsin and chymotrypsin proteolysis to the N-terminal and C-terminal regions described above, resulting in the preferential stabilization of the tetrameric form of phosphofructokinase.”
Limited proteolysis of yeast phosphofructokinase. Sequence locations of cleavage sites created by the actions of different proteinases.
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