Publication: Studies on the interaction between titin and myosin
Authors
Wang, Seu-Mei ; Chung-Jiuan Jeng ; Mu-Chien Sun
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Publisher
Murcia : F. Hernández
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DOI
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info:eu-repo/semantics/article
Description
Abstract
This study examines the interaction of titin
and mysoin. In order to analyze the domains of myosin
contributing to the binding for titin, we conducted a
solid phase binding assay. Different portions of mysoin
(heavy chains, light chains and myosin fragments ) were
coated on the microtiter wells and reacted with
biotinylated titin. Then the binding of biotinylated titin
to these polypeptides was detected by using the avidinbiotin-
peroxidase method. The results demonstrated that
light meromyosin and subfragment 1 were the major
domains of myosin interacting with titin. Titin
fragments obtained by trypsin digestion were allowed to
react with myosin in an affinity column, and the bound
fragments were isolated by an acidic elution.
Immunoblot analysis of mysoin-bound titin fragments
revealed that an A-band domain of titin was responsible
for the binding of myosin. In addition, biotinylated titin
labelled the outer A-bands and Z-bands in intact
myofibrils, thus confirming the in situ binding of titin to
myosin.
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