IN VITRO ADP-RIBOSYLATION OF AMP-DEAMINASE AND ITS EFFECT ON THE PROTECTION OF THE ADP-BINDING DOMAIN AGAINST PROTEOLYSIS
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概要
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We investigated the ADP-ribosylation of AMP-deaminase from rat and rabbit skeletal muscle by guanidino compound-specific ADP-ribosyltransferase from hen liver nuclei and its effect on the enzyme activity. Rat AMP-deaminase was ADP-ribosylated when the enzyme was incubated with ADP-ribosyl-transferase and [adenylate-^32P] NAD. Preincubation of rabbit AMP-deaminase alone resulted in a loss of ADP-dependent, but not basal, enzyme activity. If, however, the enzyme was subjected to the ADP-ribosylation system containing unlabeled NAD and ADP-ribosyltransferase, the enzyme retained the property to be activated by ADP. Electrophoretic analyses of the enzyme preparation incubated with or without the ADP-ribosylation system and subsequently further incubation with trypsin showed that the ADP-ribosylation of the enzyme protects the enzyme from proteolysis concomitant with the retention of ADP-dependent activation of the enzyme.
- 島根大学の論文
著者
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Tsuchiya Mikako
Department Of Biochemistry Faculty Of Medicine Shimane University
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Shimoyama M.
Department Of Biochemistry Shimane Medical University
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Tsuchiya M.
Department Of Biochemistry Faculty Of Medicine Shimane University
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HAROUTUNIAN A.V.
Institute of Biochemistry, Academy of Sciences of the Armenian SSR, Erevan, USSR and Department of B
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Terashima Masaharu
Department Of Biochemistry Shimane Medical University
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Haroutunian A.v.
Institute Of Biochemistry Academy Of Sciences Of The Armenian Ssr Erevan Ussr And Department Of Bioc
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