A survey of interactions made by the giant protein titin
Keyword(s):
A simple solid-phase binding assay was used to screen for interactions that the giant myofibrillar protein titin makes with other sarcomeric proteins. The titin used in the tests was purified by a modified procedure that results in isolation of approximately 20 mg relatively undegraded protein in < 24 h. In addition to the approximately 3 MDa polypeptide, bands at approximately 160 kDa and approximately 100 kDa were also consistently seen on gels. Binding of titin to myosin, C-protein, X-protein and AMP-deaminase was observed. The interaction with myosin appears to be with the light meromyosin part of the molecule.
1992 ◽
Vol 267
(17)
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pp. 11957-11963
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1988 ◽
Vol 13
(3)
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pp. 251-266
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1986 ◽
Vol 7
(6)
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pp. 550-567
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2000 ◽
Vol 10
(9)
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pp. 951-954
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2004 ◽
Vol 78
(1)
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pp. 216-223
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2001 ◽
Vol 11
(23)
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pp. 2997-3000
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