In:
Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 67, No. 4 ( 1970-12), p. 1761-1768
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 P I -protein fraction of the glutamine synthetase deadenylylating enzyme system, has S 20. w ≅ 5.1 S and a molecular weight of about 130,000. The more rapidly migrating adenylyltransferase component has S 20. w ≅ 4.0 S and a molecular weight of about 70,000. During storage at 4°C, the larger adenylyltransferase component (P I ) converts to the smaller active unit with a concomitant loss of both P I deadenylylating activity and soluble protein. It is concluded that the low-molecular weight form of the adenylyltransferase is a subunit of the deadenylylating P I -protein.
Type of Medium:
Online Resource
ISSN:
0027-8424
,
1091-6490
DOI:
10.1073/pnas.67.4.1761
Language:
English
Publisher:
Proceedings of the National Academy of Sciences
Publication Date:
1970
detail.hit.zdb_id:
209104-5
detail.hit.zdb_id:
1461794-8
SSG:
11
SSG:
12
