Abstract：
:We improved a motility assay system by using an affinity-purified antibody against the C-terminal globular domain of characean myosin. This improvement allowed us to study the sensitivity to ionic strength or the processivity of characean myosin. The sliding velocity of actin filaments on a characean myosin-coated surface was unaffected by ionic strength. This property is unlike that of skeletal or smooth muscle myosin and suggests that the binding manner of characean myosin to actin is different from that in other muscle myosins. The sliding velocity decreased when the MgADP concentration was raised. The extent of inhibition by MgADP on the motile activity of characean myosin was almost the same as in skeletal muscle or cardiac myosin. The number of sliding filaments on the characean myosin-coated surface decreased drastically with a decrease in the motor density. The motor density required to produce a successful movement of actin filament was about 200 molecules/microm(2). These results suggest that the characean myosin is not a processive motor protein.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Awata JY,Kashiyama T,Ito K,Yamamoto Kdoi
10.1016/s0022-2836(02)01469-9keywords:
subject
Has Abstractpub_date
2003-02-21 00:00:00pages
659-63issue
3eissn
0022-2836issn
1089-8638pii
S0022283602014699journal_volume
326pub_type
杂志文章abstract：:The structures of the two very closely related proteins, bovine gamma II- and gamma IVa-crystallin have been studied by means of near-ultra-violet linear dichroism spectroscopy on squeezed polyacrylamide gel systems. The crystallin spectra are discussed in terms of the spectra of the aromatic chromophores present in t...
journal_title：Journal of molecular biology
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