Artificial dimers of native actin: preparation and properties in biological functions.
With the aid of tartryl-bis-epsilon-aminocaprylazide artificial dimers were produced from F actin from rabbit striated muscle. These derivatives will not polymerize by themselves but are able to copolymerize fully with native G actin. By modification of a single side chain per dimer, this copolymerization was completely inhibited. The dimers are able to activate subfragment 1 ATPase of myosin and bind to DNase I with inactivation of the enzyme in the same manner as native G actin. Within the dimer, one ADP is immobilized and will exchange against ATP extremely slowly. The dimers do not bind to the mushroom toxin phalloidin.
Bäumert
H G
HG
Institut für Biochemie der Johann Wolfgang Goethe Universität, Frankfurt, West Germany.
Kenmoku
A
A
Middelhoff
G
G
Ortanderl
F
F
Thrun
A
A
Faulstich
H
H
Schiebler
W
W
Fasold
H
H
D000199:Actins / Q000378:metabolism*; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D003432:Cross-Linking Reagents; D066298:In Vitro Techniques; D008854:Microscopy, Electron; D009132:Muscles / Q000201:enzymology / Q000378:metabolism; D009218:Myosins / Q000378:metabolism; D010590:Phalloidine / Q000378:metabolism; D011108:Polymers; D011817:Rabbits
D000199:Actins; D003432:Cross-Linking Reagents; D011108:Polymers; D010590:Phalloidine; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; D009218:Myosins