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Calmodulin-binding peptides isolated from α-casein peptone

Published online by Cambridge University Press:  01 June 2009

Kenji Kizavva
Affiliation:
Biochemistry Laboratory, Kanebo Ltd, 5-3-28 Kotobuki-cho, Odawara 250, Japan
Keiko Naganuma
Affiliation:
Biochemistry Laboratory, Kanebo Ltd, 5-3-28 Kotobuki-cho, Odawara 250, Japan
Umeji Murakami
Affiliation:
Biochemistry Laboratory, Kanebo Ltd, 5-3-28 Kotobuki-cho, Odawara 250, Japan

Summary

Peptides that inhibit calmodulin-dependent cyclic nucleotide phosphodiesterase were isolated from a pepsin digest of α-casein. Analysis of these peptides showed that they corresponded to the αs2-casein sequences 164–179 (Leu–Lys–Lys–Ile–Ser–Gln–Arg–Tyr–Gln–Lys–Phe–Ala–Leu–Pro–Gln–Tyr), 183–206 (Val–Tyr–Gln–His–Gln–Lys–Ala–Met–Lys–Pro–Trp–Ile–Gln–Pro–Lys–Thr–Lys–Val–Ile–Pro–Tyr–Val–Arg–Tyr) and 183–207 (C-terminus, Val–Tyr–Gln–His–Gln–Lys–Ala–Met–Lys–Pro–Trp–Ile–Gln–Pro–Lys–Thr–Lys–Val–Ile–Pro–Tyr–Val–Arg–Tyr–Leu). These peptides inhibited calmodulin-induced cyclic nucleotide phosphodiesterase activity over the range 1–50 μM without affecting the basal enzyme activity. These results demonstrated that the affinities of these peptides for calmodulin are comparable to the affinities of certain endogenous neurohormones and proteins that interact with calmodulin.

Type
Original Articles
Copyright
Copyright © Proprietors of Journal of Dairy Research 1995

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References

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