Title : Interaction between caldesmon and tropomyosin in the presence and absence of smooth muscle actin.

Pub. Date : 1988 Nov 1

PMID : 3242591






7 Functional Relationships(s)
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1 The number of sulfhydryl (SH) groups in caldesmon was around 3.5 on the basis of reactivity to 5,5"-dithiobis(2-nitrobenzoate); 80% of the SH groups were labeled with pyrene. pyrene caldesmon 1 Homo sapiens
2 The fluorescence spectrum from pyrene-caldesmon showed the presence of excited monomer and dimer (excimer). pyrene caldesmon 1 Homo sapiens
3 The labeling of caldesmon with pyrene did not affect its ability to inhibit actin activation of heavy meromyosin Mg-ATPase and the release of this inhibition in the presence of Ca2+-calmodulin. pyrene caldesmon 1 Homo sapiens
4 Tropomyosin induced a change in the fluorescence spectrum of pyrene-caldesmon, indicating a conformational change associated with the interaction between caldesmon and tropomyosin. pyrene caldesmon 1 Homo sapiens
5 Tropomyosin induced a change in the fluorescence spectrum of pyrene-caldesmon, indicating a conformational change associated with the interaction between caldesmon and tropomyosin. pyrene caldesmon 1 Homo sapiens
6 The addition of tropomyosin also changed the fluorescence spectrum of pyrene-caldesmon bound to actin filaments. pyrene caldesmon 1 Homo sapiens
7 The change in the conformation of tropomyosin, caused by the interaction between caldesmon and tropomyosin, was studied with pyrene-labeled tropomyosin. pyrene caldesmon 1 Homo sapiens