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Purification and characterization of two components of acid alpha-glucosidase from pig liver.

Purification and characterization of two components of acid alpha-glucosidase from pig liver. Research Abstract Details 

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  • Purification and characterization of two components of acid alpha-glucosidase from pig liver. Abstract Text:

    k tashiroK Tashiro,t iwamasaT Iwamasa,h katoH Kato,s ogataS Ogata,m anaiM Anai,

    Acid alpha-glucosidase [EC 3.2.1.3] was purified from pig liver by a procedure including Sephadex G-100 affinity chromatography. Electrophoresis on SDS-polyacrylamide gel of the purified enzyme indicated the presence of two components with molecular weights of 73K and 64K. The two components of the enzyme were completely separated, in reasonable yield, by chromatography on a DEAE-5PW column. Both components catalyzed the hydrolysis of the alpha-1,4 and alpha-1,6 linkages of glycogen, maltose, isomaltose, dextrin, and a synthetic glucoside at acid pH. The pH optima of both components were 4.3 for maltase and glucoamylase, and 4.8 for isomaltase and dextrinase. But as to the activity on 4MU-alpha-Glc, the pH optimum of the larger component was 4.8 and that of the smaller component 5.3. The Km values of both components for 4MU-alpha-Glc, maltose, glycogen, isomaltose, and dextrin were 1.0 X 10(-4) M, 9.1 X 10(-3) M, 16.7 mg/ml, 6.7 X 10(-2) M, and 12.5 mg/ml, respectively. Erythritol, Tris, and turanose inhibited the two components competitively. The Ki values of the larger component were 5.0 X 10(-2) M, 13.3 X 10(-3) M, and 3.2 X 10(-3) M, and those of the smaller component were 2.5 X 10(-2) M, 6.1 X 10(-3) M, and 4.7 X 10(-3) M, for erythritol, Tris, and turanose, respectively.

    Purification and characterization of two components of acid alpha-glucosidase from pig liver. Publishing Authors By Initials

    k tashiroK Tashiro,t iwamasaT Iwamasa,h katoH Kato,s ogataS Ogata,m anaiM Anai,

    For similar enzymes and coenzymes: enzymes: hydrolases: glycoside hydrolases: glucosidases: alpha-glucosidases research abstracts see: enzymes and coenzymes: enzymes: hydrolases: glycoside hydrolases: glucosidases: alpha-glucosidases research

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    Purification and characterization of two components of acid alpha-glucosidase from pig liver. Journal Published:

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

    Journal: Journal of biochemistry

    VOLUME: 99

    Page Numbers: 693-701

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Mar

    YEAR: 1986

    Purification and characterization of two components of acid alpha-glucosidase from pig liver. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Purification and characterization of two components of acid alpha-glucosidase from pig liver. Keywords Mesh Terms:

    KEYWORDS: alpha-Glucosidases

    MESH TERMS: isolation & purification

    Chemical & Substance for Abstract: Purification and characterization of two components of acid alpha-glucosidase from pig liver. Information

    Substance Name: alpha-Glucosidases

    Registry Number: EC 3.2.1.20

    Grant and Affiliation Information for Purification and characterization of two components of acid alpha-glucosidase from pig liver.

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    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    MEDLINETA: J Biochem

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