Cap Z( 36 32) is a contaminant and the major inhibitor of actin neiwork formation in conventional actin preparations

James F. Casella; Donna J. Maack

doi:10.1016/0006-291X(87)91366-0

Cap Z_{( 36 32)} is a contaminant and the major inhibitor of actin neiwork formation in conventional actin preparations

James F. Casella, Donna J. Maack

School of Medicine

Research output: Contribution to journal › Article › peer-review

9 Scopus citations

Abstract

Previous studies have demonstrated that conventional actin preparations contain a potent factor which reduces the low shear viscosity of actin filaments (1). In this paper we demonstrate that Cap Z_{( 36 32)}, a recently described protein from skeletal muscle that caps the barbed end of actin filaments and localizes to the Z-line of skeletal muscle (2,3), is the major factor affecting the low shear viscosity of actin prepared from muscle as described by Spudich and Watt (4).

Original language	English (US)
Pages (from-to)	625-630
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	145
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(87)91366-0
State	Published - May 29 1987

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/0006-291X(87)91366-0

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title = "Cap Z( 36 32) is a contaminant and the major inhibitor of actin neiwork formation in conventional actin preparations",

abstract = "Previous studies have demonstrated that conventional actin preparations contain a potent factor which reduces the low shear viscosity of actin filaments (1). In this paper we demonstrate that Cap Z( 36 32), a recently described protein from skeletal muscle that caps the barbed end of actin filaments and localizes to the Z-line of skeletal muscle (2,3), is the major factor affecting the low shear viscosity of actin prepared from muscle as described by Spudich and Watt (4).",

author = "Casella, {James F.} and Maack, {Donna J.}",

note = "Funding Information: This work was supported by funds from the Aaron Straus and Lillie Straus Foundation, Inc., the Marion J. Gallagher Foundation, Inc., N.I.H. Clinical Investigator mard SK08 HLO1341 (to J.F.C.), and N.I.H. Biom&iiti Research Support Grant RR5378 to the Johns Hopkins School of Medicine. The authors wish to thank: Ms. Phyllis O'Neill and Ms. Jacqueline Hollands for help with the preparation of this manuscript, and Dover Poultry for providing the chickens used in this study.",

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T1 - Cap Z( 36 32) is a contaminant and the major inhibitor of actin neiwork formation in conventional actin preparations

AU - Casella, James F.

AU - Maack, Donna J.

N1 - Funding Information: This work was supported by funds from the Aaron Straus and Lillie Straus Foundation, Inc., the Marion J. Gallagher Foundation, Inc., N.I.H. Clinical Investigator mard SK08 HLO1341 (to J.F.C.), and N.I.H. Biom&iiti Research Support Grant RR5378 to the Johns Hopkins School of Medicine. The authors wish to thank: Ms. Phyllis O'Neill and Ms. Jacqueline Hollands for help with the preparation of this manuscript, and Dover Poultry for providing the chickens used in this study.

PY - 1987/5/29

Y1 - 1987/5/29

N2 - Previous studies have demonstrated that conventional actin preparations contain a potent factor which reduces the low shear viscosity of actin filaments (1). In this paper we demonstrate that Cap Z( 36 32), a recently described protein from skeletal muscle that caps the barbed end of actin filaments and localizes to the Z-line of skeletal muscle (2,3), is the major factor affecting the low shear viscosity of actin prepared from muscle as described by Spudich and Watt (4).

AB - Previous studies have demonstrated that conventional actin preparations contain a potent factor which reduces the low shear viscosity of actin filaments (1). In this paper we demonstrate that Cap Z( 36 32), a recently described protein from skeletal muscle that caps the barbed end of actin filaments and localizes to the Z-line of skeletal muscle (2,3), is the major factor affecting the low shear viscosity of actin prepared from muscle as described by Spudich and Watt (4).

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Cap Z_{( 36 32)} is a contaminant and the major inhibitor of actin neiwork formation in conventional actin preparations

Abstract

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