KMID : 0366319910110040241
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Biochemistry and Molecular Biology News 1991 Volume.11 No. 4 p.241 ~ p.242
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Magnetotactic Bacteria
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Abstract
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The catalytic activity of the phosphorylase kinase resides with i subunit. The r subunit has been isolated from the phosphorylase kinase holoenzyme using harsh denaturing conditions and the isolate subunit has been reactivated. The reactivated r subunit has been characterized. The cDNAs of the i subunit were cloned and the cDNA has been used for a better understanding of the molecular basis of Phk deficiencies. The Phk--c cDNA were obtain the native, active -c subunit. Functional domains of the t subunit have been studied and expect to be studied more using cDNA mutation. The complete purification of the expressed -c subunit need to be accomplished for further studies.
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KEYWORD
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