Identification of peptides in wheat germ hydrolysate that demonstrate calmodulin-dependent protein kinase II inhibitory activity
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文摘

Wheat germ hydrolyzed by thermolysin inhibited in vitro CaMK II activity.

Trp-Val and Trp-Ile were identified as CaMK II inhibitor.

The N-terminal Trp residue is essential for the inhibitory effect.

Trp-Val and Trp-Ile inhibited the binding of the Ca2+-CaM complex to CaMK II.

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