Calcium binding to the low affinity sites in troponin C induces conformational changes in the high affinity domain. A possible route of information transfer in activation of muscle contraction.

Artigo Acesso aberto Revisado por pares

Calcium binding to the low affinity sites in troponin C induces conformational changes in the high affinity domain. A possible route of information transfer in activation of muscle contraction.

1986; Elsevier BV; Volume: 261; Issue: 2 Linguagem: Inglês

10.1016/s0021-9258(17)36135-5

ISSN

1083-351X

Autores

Zenon Grabarek, Paul C. Leavis, J. Gergely,

Tópico(s)

Cardiac electrophysiology and arrhythmias

Resumo

We havestudied Ca2+-induced changes in the region C88-100 by monitoring the fluorescence of troponin C (TnC) labeled at Cys-98 with 5-(iodoac-etamidoethy1)aminonaphthalene-l-sulfonic acid.Equilibrium titration of the labeled TnC with Ca" indicates that the probe is sensitive to binding to both classes of sites in free TnC as well as in its complex with TnI.

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Calcium binding to the low affinity sites in troponin C induces conformational changes in the high affinity domain. A possible route of information transfer in activation of muscle contraction.