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KMID : 0364519980100020199
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Dong-A Journal Medicine
1998 Volume.10 No. 2 p.199 ~ p.204
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High Molecular Weight Poly (ADP-ribosyl)toted Proteins Are Not Derived from 110 kD Poly (ADP-ribose) Synthase
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Hwang Tae-Ho
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Abstract
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In order to resolve a novel question as to whether or not high molecular weight poly
(ADP-ribosyl)toted proteins are all derived from autocatalysis of poly (ADP-ribose)
synthase, the bulk[32P]-labelled poly (ADP-ribosyl)acted proteins were
isolated by DEAE-cellulose column chromatography. Since they were labelled by high
[32P]-labelling techniques using HeLa cells, ultramicro-analysis was
possible to study poly (ADP-ribose) structures. This preparation was further fractionated
by two dimensional gel electrophoresis, the first dimension by electrofocusing at pH 3∼7
and the second dimension on 7% SDS-polyacrlamide gel. All the high molecular weight
species were discretely separated showing different pl’s in the range 3∼5. There were
two pl groups of the proteins. One was a strongly acidic group which were separated in
a pH range 3∼4. The second was an intermediate acidic group which were separated in
a pH range 4∼5. Therefore, it was impossible to support the unitarian theory of high
molecular weight poly (ADP-ribosyl)acted proteins which are all derived from the single
parent molecular species of 110kD poly (ADP-ribose) synthase. By analysis of
constituent poly (ADP-ribose), it became clear that all the molecular species contain a
common structure composed of terminal 5’-AMP, internal isoADP-ribose repeating units
and branch phosphoribosyl isoADP-ribose.
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KEYWORD
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Isoelectric focusing, Isoelectric point, Strong1y acidic poly(ADP-ribose), Branched poly(ADP-ribose), Iso-ADP-ribose,
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