Brain myo-inositol monophosphatase: Activity of the single subunit in a dimeric enzyme

F. Kwok; Chun Lap Samuel Lo; J. E. Churchich

Brain myo-inositol monophosphatase: Activity of the single subunit in a dimeric enzyme

F. Kwok, Chun Lap Samuel Lo, J. E. Churchich

Research output: Journal article publication › Journal article › Academic research › peer-review

Abstract

Reversible dissociation of the dimeric structure of brain myo-inositol monophosphatase into subunits was attained by the addition of guanidine-HCl (4M). The molecular mass of the subunits (29 KDa) was determined by HPLC chromatography. Separation of the processes of refolding and association of the monomeric species was achieved by attaching the protein subunits to a rigid matrix (Affi-gel 15). The matrix-bound monomer is determined to be catalytically active, indicating that monomeric subunit of the phosphatase is capable of conducting independent catalysis.

Original language	English
Pages (from-to)	325-330
Number of pages	6
Journal	Biochemistry and Molecular Biology International
Volume	32
Issue number	2
Publication status	Published - 25 Mar 1994

ASJC Scopus subject areas

Biochemistry
Genetics
Molecular Biology

Cite this

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abstract = "Reversible dissociation of the dimeric structure of brain myo-inositol monophosphatase into subunits was attained by the addition of guanidine-HCl (4M). The molecular mass of the subunits (29 KDa) was determined by HPLC chromatography. Separation of the processes of refolding and association of the monomeric species was achieved by attaching the protein subunits to a rigid matrix (Affi-gel 15). The matrix-bound monomer is determined to be catalytically active, indicating that monomeric subunit of the phosphatase is capable of conducting independent catalysis.",

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N2 - Reversible dissociation of the dimeric structure of brain myo-inositol monophosphatase into subunits was attained by the addition of guanidine-HCl (4M). The molecular mass of the subunits (29 KDa) was determined by HPLC chromatography. Separation of the processes of refolding and association of the monomeric species was achieved by attaching the protein subunits to a rigid matrix (Affi-gel 15). The matrix-bound monomer is determined to be catalytically active, indicating that monomeric subunit of the phosphatase is capable of conducting independent catalysis.

AB - Reversible dissociation of the dimeric structure of brain myo-inositol monophosphatase into subunits was attained by the addition of guanidine-HCl (4M). The molecular mass of the subunits (29 KDa) was determined by HPLC chromatography. Separation of the processes of refolding and association of the monomeric species was achieved by attaching the protein subunits to a rigid matrix (Affi-gel 15). The matrix-bound monomer is determined to be catalytically active, indicating that monomeric subunit of the phosphatase is capable of conducting independent catalysis.

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M3 - Journal article

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JO - Biochemistry and Molecular Biology International

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ER -

Brain myo-inositol monophosphatase: Activity of the single subunit in a dimeric enzyme

Abstract

ASJC Scopus subject areas

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