There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.
Abstract
One of the reactive thiols in the myosin head, SH1, was covalently labeled with a
biotin derivative, N-iodoacetyl-N'-biotinylhexylenediamine. When 50% of the SH1 thiol
was modified with the biotin reagent as judged from measurements of ATPase activities,
the biotinylated myosin bound one mole of avidin per mole of myosin at the saturating
level. The avidin-myosin complex was readily formed in the presence of MgADP or MgATP.
Peptide maps of the biotinylated myosin revealed that SH1 is actually the site of
biotinylation with N-iodoacetyl-N'-biotinylhexylenediamine. Electron microscopic examination
of the avidin-myosin complex showed that the attachment site of avidin on the myosin
head is 130 A from the head-rod junction, indicating that the SH1 thiol is located
there.