Shannon Hitchcock

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The bindings of troponin components to actin and tropomyosin has been studied by cosedimentation with actin and affinity chromatography. It is shown that troponin binds to actin and tropomyosin in the presence and absence of calcium but the binding to actin is sensitive to ionic strength. Troponin-I + C binds to actin-tropomyosin in the absence of calcium(More)
Deoxyribonuclease I (DNase I) forms a 1:1 complex with globular actin (G-actin) and also will depolymerize filamentous actin (F-actin) to form a 1:1 complex. The effect of DNase I on the exchange of the actin nucleotide has been investigated. When DNase I is added to G-actin, the rate of nucleotide exchange is decreased from 1.16 +/- 0.25 X 10(-4) s-1 to(More)
The topology of troponin, the calcium binding regulatory protein in muscle, has been studied by cross-linking with different length dimethylimido esters. The results show that the three components of troponin are close to each other and that the troponin-I and -T are preferentially cross-linked being 0.6 nm or less apart. The largest cross-linked product is(More)
In the past several years actomyosin contractile systems have been related to many types of cell movement and other functions such as cytoplasmic streaming, cytokinesis, blood clot retraction, and phagocytosis. The evidence for the presence of actin and myosin in nonmuscle cells is now widespread and has been the subject of a recent review (85) and two(More)