Abstract:
:In the presence of the nucleotide analog adenosine 5'-[gamma-thio]triphosphate (ATP[gamma S]), effects of Ca2+ on stiffness and equatorial x-ray diffraction patterns of single skinned fibers of the rabbit psoas muscle were studied. It is shown that cross-bridges in the presence of ATP[gamma S] have properties of the weak-binding states of the ATP hydrolysis cycle. Raising the Ca2+ concentration up to pCa 4.5 has little effect on actin affinity of cross-bridges in the presence of ATP[gamma S]. However, the rate constants for cross-bridge dissociation and reassociation from and to actin are reduced by about 2 orders of magnitude. In addition, nucleotide affinity of the cross-bridge is much smaller at high Ca2+ concentrations. Implications for interpretation of fiber stiffness recorded during isotonic shortening and the rising phase of a tetanus are discussed.
journal_name
Proc Natl Acad Sci U S Aauthors
Kraft T,Yu LC,Kuhn HJ,Brenner Bdoi
10.1073/pnas.89.23.11362keywords:
subject
Has Abstractpub_date
1992-12-01 00:00:00pages
11362-6issue
23eissn
0027-8424issn
1091-6490journal_volume
89pub_type
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