TY - JOUR
T1 - Actin crosslinked with glutaraldehyde
T2 - Evidence to suggest an active role for actin in the regulatory mechanism
AU - Poo, W. J.
AU - Hartshorne, D. J.
PY - 1976/5/17
Y1 - 1976/5/17
N2 - Actin crosslinked with glutaraldehyde retains the ability to activate the Mg2+-ATPase activity of heavy meromyosin subfragment 1, but the resultant ATPase activity is not controlled by the regulatory proteins, troponin and tropomyosin. Fluorescent energy transfer measurements imply that the crosslinked actin is frozen in the active state. These results indicate that the conformation of actin is important in the regulatory mechanism, and suggest that actin plays a more active role in this mechanism than thought previously.
AB - Actin crosslinked with glutaraldehyde retains the ability to activate the Mg2+-ATPase activity of heavy meromyosin subfragment 1, but the resultant ATPase activity is not controlled by the regulatory proteins, troponin and tropomyosin. Fluorescent energy transfer measurements imply that the crosslinked actin is frozen in the active state. These results indicate that the conformation of actin is important in the regulatory mechanism, and suggest that actin plays a more active role in this mechanism than thought previously.
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U2 - 10.1016/0006-291X(76)91060-3
DO - 10.1016/0006-291X(76)91060-3
M3 - Article
C2 - 132931
AN - SCOPUS:0017079923
SN - 0006-291X
VL - 70
SP - 406
EP - 412
JO - Biochemical and biophysical research communications
JF - Biochemical and biophysical research communications
IS - 2
ER -