| Literature DB >> 2978377 |
H G Bäumert1, A Kenmoku, G Middelhoff, F Ortanderl, A Thrun, H Faulstich, W Schiebler, H Fasold.
Abstract
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.Entities:
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Year: 1988 PMID: 2978377 DOI: 10.1007/bf01024875
Source DB: PubMed Journal: J Protein Chem ISSN: 0277-8033