Identification of a third form of protein phosphatase 1 in rabbit skeletal muscle that is associated with myosin

Alexander A K Chisholm; Philip Cohen

doi:10.1016/0167-4889(88)90032-8

Identification of a third form of protein phosphatase 1 in rabbit skeletal muscle that is associated with myosin

Alexander A K Chisholm, Philip Cohen

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

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Abstract

A third form of protein phosphatase 1 has been identified in skeletal muscle which is distinct from the species composed of the catalytic subunit complexed to the glycogen-binding subunit (protein phosphatase 1_G) or inhibitor-2 (protein phosphatase 1_I). The third form has an apparent molecular mass of 110 kDa, is not immunoprecipitated by antibody prepared against the glycogen-binding subunit, does not interact with glycogen and is devoid of inhibitor-2. It is tightly bound to myosin and is therefore termed protein phosphatase 1_M.

Original language	English
Pages (from-to)	392-400
Number of pages	9
Journal	BBA - Molecular Cell Research
Volume	968
Issue number	3
DOIs	https://doi.org/10.1016/0167-4889(88)90032-8
Publication status	Published - 11 Mar 1988

Keywords

(Skeletal muscle)
Glycogen binding
Glycogen metabolism
Myosin binding
Protein phosphatase 1

ASJC Scopus subject areas

Biophysics
Cell Biology
Molecular Biology

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abstract = "A third form of protein phosphatase 1 has been identified in skeletal muscle which is distinct from the species composed of the catalytic subunit complexed to the glycogen-binding subunit (protein phosphatase 1G) or inhibitor-2 (protein phosphatase 1I). The third form has an apparent molecular mass of 110 kDa, is not immunoprecipitated by antibody prepared against the glycogen-binding subunit, does not interact with glycogen and is devoid of inhibitor-2. It is tightly bound to myosin and is therefore termed protein phosphatase 1M.",

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AU - Cohen, Philip

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N2 - A third form of protein phosphatase 1 has been identified in skeletal muscle which is distinct from the species composed of the catalytic subunit complexed to the glycogen-binding subunit (protein phosphatase 1G) or inhibitor-2 (protein phosphatase 1I). The third form has an apparent molecular mass of 110 kDa, is not immunoprecipitated by antibody prepared against the glycogen-binding subunit, does not interact with glycogen and is devoid of inhibitor-2. It is tightly bound to myosin and is therefore termed protein phosphatase 1M.

AB - A third form of protein phosphatase 1 has been identified in skeletal muscle which is distinct from the species composed of the catalytic subunit complexed to the glycogen-binding subunit (protein phosphatase 1G) or inhibitor-2 (protein phosphatase 1I). The third form has an apparent molecular mass of 110 kDa, is not immunoprecipitated by antibody prepared against the glycogen-binding subunit, does not interact with glycogen and is devoid of inhibitor-2. It is tightly bound to myosin and is therefore termed protein phosphatase 1M.

KW - (Skeletal muscle)

KW - Glycogen binding

KW - Glycogen metabolism

KW - Myosin binding

KW - Protein phosphatase 1

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JO - Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

JF - Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

IS - 3

ER -

Identification of a third form of protein phosphatase 1 in rabbit skeletal muscle that is associated with myosin

Abstract

Keywords

ASJC Scopus subject areas

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