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- W75074927 abstract "Glucose-6-phosphate phosphohydrolase , an enzyme of the microsomal fraction, is a major intermediate in the mobilization of glucose from calf liver cells. A defect in the hydrolytic function of this enzyme is responsible for Glycogen storage disease Type I. This chapter presents a study that was undertaken to purify this membrane-bound enzyme using the techniques of affinity chromatography. Microsomes were prepared from human liver samples obtained at autopsy by the method of Garland and Cori. Wash buffers were supplemented with 0.2% sodium deoxycholate, which disrupted microsomes and increased enzyme activity 10-fold. These microsomes were transferred to a DEAE-Cellulose column . Bound proteins were eluted from this column by a NaCl gradient to 0.5 M. Two elution peaks were resolved. Protein eluted at high salt was found to have high activity representing a purification of approximately 20-fold, while recovering some 10% of the total enzyme activity. Preliminary studies using glucose-6-phosphate covalently linked to a Sepharose 6B column gave an additional measure of purification." @default.
- W75074927 created "2016-06-24" @default.
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- W75074927 date "1982-01-01" @default.
- W75074927 modified "2023-09-26" @default.
- W75074927 title "THE PURIFICATION OF MICROSOMAL GLUCOSE-6-PHOSPHATASE FROM HUMAN LIVER: AIDS TO THE STUDY OF GLYCOGEN STORAGE DISEASE" @default.
- W75074927 cites W2044661596 @default.
- W75074927 doi "https://doi.org/10.1016/b978-0-12-045560-7.50078-0" @default.
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