Comparative Purification Of Myocardial Myosin And Antigenic Specificity Of The Two Light Chains

J. Wikman-Coffelt; R. Zelis; C. Fenner; D. T. Mason

doi:10.1080/00327487308061528

Comparative Purification Of Myocardial Myosin And Antigenic Specificity Of The Two Light Chains

J. Wikman-Coffelt, R. Zelis, C. Fenner, D. T. Mason

Department of Medicine

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

34 Scopus citations

Abstract

Dog myocardial myosin preparations, purified according to the procedures presented here, utilizing either one or two (NH₄)₂SO₄fractionations, contained no major contaminants which could be detected by disc gel electrophoresis, and exhibited high myosin ATPase activity. The low molecular weight components (light chains) were dissociated from the rest of the molecule by denaturing with urea; the chains were further purified by column chromatography. Procedures were a modification of those used for purification of skeletal muscle myosin light chains. According to immunoanalyses the two myocardial myosin light chains showed antigenic specificity.

Original language	English (US)
Pages (from-to)	439-449
Number of pages	11
Journal	Preparative Biochemistry
Volume	3
Issue number	5
DOIs	https://doi.org/10.1080/00327487308061528
State	Published - Jan 1 1973

All Science Journal Classification (ASJC) codes

Biochemistry
Genetics

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10.1080/00327487308061528

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title = "Comparative Purification Of Myocardial Myosin And Antigenic Specificity Of The Two Light Chains",

abstract = "Dog myocardial myosin preparations, purified according to the procedures presented here, utilizing either one or two (NH4)2SO4fractionations, contained no major contaminants which could be detected by disc gel electrophoresis, and exhibited high myosin ATPase activity. The low molecular weight components (light chains) were dissociated from the rest of the molecule by denaturing with urea; the chains were further purified by column chromatography. Procedures were a modification of those used for purification of skeletal muscle myosin light chains. According to immunoanalyses the two myocardial myosin light chains showed antigenic specificity.",

author = "J. Wikman-Coffelt and R. Zelis and C. Fenner and Mason, {D. T.}",

note = "Funding Information: Supported by Research Program Project Grant HL-14780 and Health Sciences Advancement Award RR-06138 from the National Institutes of Health, and the Sacramento-Yolo-Sierra Heart Association.",

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AU - Zelis, R.

AU - Fenner, C.

AU - Mason, D. T.

N1 - Funding Information: Supported by Research Program Project Grant HL-14780 and Health Sciences Advancement Award RR-06138 from the National Institutes of Health, and the Sacramento-Yolo-Sierra Heart Association.

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N2 - Dog myocardial myosin preparations, purified according to the procedures presented here, utilizing either one or two (NH4)2SO4fractionations, contained no major contaminants which could be detected by disc gel electrophoresis, and exhibited high myosin ATPase activity. The low molecular weight components (light chains) were dissociated from the rest of the molecule by denaturing with urea; the chains were further purified by column chromatography. Procedures were a modification of those used for purification of skeletal muscle myosin light chains. According to immunoanalyses the two myocardial myosin light chains showed antigenic specificity.

AB - Dog myocardial myosin preparations, purified according to the procedures presented here, utilizing either one or two (NH4)2SO4fractionations, contained no major contaminants which could be detected by disc gel electrophoresis, and exhibited high myosin ATPase activity. The low molecular weight components (light chains) were dissociated from the rest of the molecule by denaturing with urea; the chains were further purified by column chromatography. Procedures were a modification of those used for purification of skeletal muscle myosin light chains. According to immunoanalyses the two myocardial myosin light chains showed antigenic specificity.

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Comparative Purification Of Myocardial Myosin And Antigenic Specificity Of The Two Light Chains

Abstract

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