Reconstitution of urea-dissociated subunits of a pig heart phosphoprotein phosphatase.

Reconstitution of urea-dissociated subunits of a pig heart phosphoprotein phosphatase. Research Abstract Details 

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Reconstitution of urea-dissociated subunits of a pig heart phosphoprotein phosphatase. Abstract Text:

M Imazu,T Imaoka,H Usui,N Kinohara,M Takeda,

Pig heart phosphoprotein phosphatase [phosphoprotein phosphophydrolase, EC 3.1.3.16] of Mr 224,000 was dissociated by gel-filtration on Sephacryl S-300, into an active subunit (alpha subunit) of Mr 31,000 and inactive subunits of higher molecular weight in the presence of 6 M urea. After the removal of urea, these subunits reassociated, forming two enzyme forms of Mr 237,000 (Form 1) and Mr 123,000 (Form 2). Form 2 was produced by association of the alpha subunit with an inactive subunit (beta subunit) of Mr 80,000, while Form 1 was formed by combination of the alpha subunit with a complex of inactive subunits which was eluted from a Sephadex G-150 column in fractions of molecular weight range greater than 80,000. The dissociation and reassociation of the subunits of Form 1 by the same urea method produced not only Form 1, but also significant amounts of Form 2, indicating that the inactive subunits of Form 1 were a complex of the beta subunit with another inactive subunit(s). The molecular parameters and other properties of Form 1 were very close to those of the original enzyme. By the conversion of Form 1 to Form 2, the activities of Form 1 towards phosphorylase a and glycogen synthetase b were enhanced 2-3 fold with no significant change in activity towards P-H1 histone or in response to the stimulatory effect of Mg(CH3COO)2 on the dephosphorylation of P-H2B histone. However, removal of the beta subunit from From 2 resulted in strong suppression of activity towards P-H1 histone and response to the salt effect with lesser effects on the activities of Form 2 towards phosphorylase a and glycogen synthase b.

Reconstitution of urea-dissociated subunits of a pig heart phosphoprotein phosphatase. Publishing Authors By Initials

M Imazu,T Imaoka,H Usui,N Kinohara,M Takeda,

For similar organic chemicals: urea research abstracts see: organic chemicals: urea research

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Reconstitution of urea-dissociated subunits of a pig heart phosphoprotein phosphatase. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 90

Page Numbers: 851-62

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Sep

YEAR: 1981

Reconstitution of urea-dissociated subunits of a pig heart phosphoprotein phosphatase. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Reconstitution of urea-dissociated subunits of a pig heart phosphoprotein phosphatase. Keywords Mesh Terms:

KEYWORDS: Urea

MESH TERMS: pharmacology

Chemical & Substance for Abstract: Reconstitution of urea-dissociated subunits of a pig heart phosphoprotein phosphatase. Information

Substance Name: Phosphoprotein Phosphatases

Registry Number: EC 3.1.3.16

Grant and Affiliation Information for Reconstitution of urea-dissociated subunits of a pig heart phosphoprotein phosphatase.

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Country: JAPAN

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MEDLINETA: J Biochem

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