Binding of myosin cross-bridges to thin filaments of rabbit skeletal muscle

O. A. Andreev; J. Borejdo

doi:10.1006/bbrc.1999.0319

Binding of myosin cross-bridges to thin filaments of rabbit skeletal muscle

O. A. Andreev, J. Borejdo

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Abstract

Cross-linking of myosin subfragment 1 (S1) with a molar excess of actin in vitro reveals the presence of an actin-S1-actin complex. It is absolutely essential that actin be present in molar excess over S1 so that the decoration of F-actin with S1 be incomplete. However, the excess of actin may not be available in the overlap zone of sarcomeres of skeletal muscle. We therefore found it necessary to test for the presence of the actin-S1-actin complex in vivo. Myofibrils from rabbit skeletal muscle were reacted with zero-length cross-linker, the products were resolved by polyacrylamide gel electrophoresis and analyzed by Western blots using antibodies against actin and against heavy and light chains of myosin. The cross-linking produced the evidence of formation of actin-S1-actin complex.

Original language	English
Pages (from-to)	628-631
Number of pages	4
Journal	Biochemical and Biophysical Research Communications
Volume	258
Issue number	3
DOIs	https://doi.org/10.1006/bbrc.1999.0319
State	Published - 19 May 1999

Keywords

Actin and myosin
Contractility
Cross-linking
Skeletal muscle

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10.1006/bbrc.1999.0319

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title = "Binding of myosin cross-bridges to thin filaments of rabbit skeletal muscle",

abstract = "Cross-linking of myosin subfragment 1 (S1) with a molar excess of actin in vitro reveals the presence of an actin-S1-actin complex. It is absolutely essential that actin be present in molar excess over S1 so that the decoration of F-actin with S1 be incomplete. However, the excess of actin may not be available in the overlap zone of sarcomeres of skeletal muscle. We therefore found it necessary to test for the presence of the actin-S1-actin complex in vivo. Myofibrils from rabbit skeletal muscle were reacted with zero-length cross-linker, the products were resolved by polyacrylamide gel electrophoresis and analyzed by Western blots using antibodies against actin and against heavy and light chains of myosin. The cross-linking produced the evidence of formation of actin-S1-actin complex.",

keywords = "Actin and myosin, Contractility, Cross-linking, Skeletal muscle",

author = "Andreev, {O. A.} and J. Borejdo",

note = "Funding Information: We thank Dr S. Lowey for antibodies. This work was supported by Grant RO1 AR40095 from NIH.",

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T1 - Binding of myosin cross-bridges to thin filaments of rabbit skeletal muscle

AU - Andreev, O. A.

AU - Borejdo, J.

N1 - Funding Information: We thank Dr S. Lowey for antibodies. This work was supported by Grant RO1 AR40095 from NIH.

PY - 1999/5/19

Y1 - 1999/5/19

N2 - Cross-linking of myosin subfragment 1 (S1) with a molar excess of actin in vitro reveals the presence of an actin-S1-actin complex. It is absolutely essential that actin be present in molar excess over S1 so that the decoration of F-actin with S1 be incomplete. However, the excess of actin may not be available in the overlap zone of sarcomeres of skeletal muscle. We therefore found it necessary to test for the presence of the actin-S1-actin complex in vivo. Myofibrils from rabbit skeletal muscle were reacted with zero-length cross-linker, the products were resolved by polyacrylamide gel electrophoresis and analyzed by Western blots using antibodies against actin and against heavy and light chains of myosin. The cross-linking produced the evidence of formation of actin-S1-actin complex.

AB - Cross-linking of myosin subfragment 1 (S1) with a molar excess of actin in vitro reveals the presence of an actin-S1-actin complex. It is absolutely essential that actin be present in molar excess over S1 so that the decoration of F-actin with S1 be incomplete. However, the excess of actin may not be available in the overlap zone of sarcomeres of skeletal muscle. We therefore found it necessary to test for the presence of the actin-S1-actin complex in vivo. Myofibrils from rabbit skeletal muscle were reacted with zero-length cross-linker, the products were resolved by polyacrylamide gel electrophoresis and analyzed by Western blots using antibodies against actin and against heavy and light chains of myosin. The cross-linking produced the evidence of formation of actin-S1-actin complex.

KW - Actin and myosin

KW - Contractility

KW - Cross-linking

KW - Skeletal muscle

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EP - 631

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 3

ER -

Binding of myosin cross-bridges to thin filaments of rabbit skeletal muscle

Abstract

Keywords

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