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. 1970 Dec;67(4):1761–1768. doi: 10.1073/pnas.67.4.1761

Adenosine Triphosphate: Glutamine Synthetase Adenylyltransferase of Escherichia coli: Two Active Molecular Forms

S Barbara Hennig 1,*, Wayne B Anderson 1,†, Ann Ginsburg 1
PMCID: PMC283424  PMID: 4923119

Abstract

Two active forms of purified ATP:glutamine synthetase adenylyl-transferase from Escherichia coli are apparent on polyacrylamide gel electrophoresis at pH 8. The slower migrating component, which is identical to the PI-protein fraction of the glutamine synthetase deadenylylating enzyme system, has S20.w ≅ 5.1 S and a molecular weight of about 130,000. The more rapidly migrating adenylyltransferase component has S20.w ≅ 4.0 S and a molecular weight of about 70,000. During storage at 4°C, the larger adenylyltransferase component (PI) converts to the smaller active unit with a concomitant loss of both PI deadenylylating activity and soluble protein. It is concluded that the low-molecular weight form of the adenylyltransferase is a subunit of the deadenylylating PI-protein.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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