Quantitation by fast-atom bombardment/mass-analysed ion kinetic energy spectrometry: Kinetic analysis of cyclic nucleotide phosphodiesterase activity

1989 ◽  
Vol 3 (6) ◽  
pp. 178-182 ◽  
Author(s):  
R. P. Newton ◽  
T. J. Walton ◽  
A. G. Brenton ◽  
E. E. Kingston ◽  
F. M. Harris
Keyword(s):  
Kinetic Energy ◽  
Kinetic Analysis ◽  
Cyclic Nucleotide ◽  
Fast Atom Bombardment ◽  
Cyclic Nucleotide Phosphodiesterase ◽  
Phosphodiesterase Activity ◽  
Ion Kinetic Energy

Calmodulin-binding peptides isolated from α-casein peptone

1995 ◽  
Vol 62 (4) ◽  
pp. 587-592 ◽  
Author(s):  
Kenji Kizavva ◽  
Keiko Naganuma ◽  
Umeji Murakami
Keyword(s):  
Enzyme Activity ◽  
Cyclic Nucleotide ◽  
Cyclic Nucleotide Phosphodiesterase ◽  
Phosphodiesterase Activity ◽  
Calmodulin Binding ◽  
C Terminus ◽  
Binding Peptides

SUMMARYPeptides 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.

Sign in / Sign up

Export Citation Format

Share Document