ATPase activities of the two cross-linked species of actin and myosin.
We describe cross-linking conditions for myosin subfragment-1 and actin with 1-ethyl-3-[3-(dimethylamino)propyl]carbodiimide, with which the compositions of cross-linked species can be altered. The specific Mg-ATPase activity of cross-linked subfragment-1 in these preparations was almost the same in spite of the differences in the compositions of the cross-linked species. This suggests that the two kinds of cross-linked species have almost the same ATPase activity, and that the cross-linking at these different sites nearly equally facilitates the formation of the strong binding state which accompanies the release of ADP and Pi.
Yamamoto
K
K
Department of Bioengineering, Soka University, Tokyo.
D000199:Actins / Q000737:chemistry*; D000251:Adenosine Triphosphatases / Q000737:chemistry*; D000255:Adenosine Triphosphate / Q000737:chemistry; D000818:Animals; D002645:Chickens; D003432:Cross-Linking Reagents; D004591:Electrophoresis, Polyacrylamide Gel; D005022:Ethyldimethylaminopropyl Carbodiimide; D006868:Hydrolysis; D009132:Muscles / Q000737:chemistry / Q000201:enzymology; D015879:Myosin Subfragments / Q000737:chemistry*; D011485:Protein Binding
D000199:Actins; D003432:Cross-Linking Reagents; D015879:Myosin Subfragments; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; D005022:Ethyldimethylaminopropyl Carbodiimide