AFFINITY CHROMATOGRAPHY OF TRYPTOPHAN SYNTHASE FROM E. COLI

作者: H.P. Gschwind , K. Kirschner

DOI: 10.1016/B978-0-08-022632-3.50013-1

关键词:

摘要: Nonreactive substrate analogues of indoleglycerol phosphate have been synthesized, starting from tryptophanol phosphate. The parent compound does not inhibit tryptophan synthase E. coli. However, a number N-acyl derivatives are excellent competitive inhibitors. These compounds the basis Sepharose used for affinity chromatography synthase.

参考文章(10)
Osao Adachi, Leonard D. Kohn, Edith Wilson Miles, Crystalline α2β2 Complexes of Tryptophan Synthetase of Escherichia coli: A COMPARISON BETWEEN THE NATIVE COMPLEX AND THE RECONSTITUTED COMPLEX Journal of Biological Chemistry. ,vol. 249, pp. 7756- 7763 ,(1974) , 10.1016/S0021-9258(19)42032-2
Pádraig O'Carra, Standish Barry, Tadhg Griffin, Interfering and complicating adsorption effects in bioaffinity chromatography. Methods in Enzymology. ,vol. 34, pp. 108- 126 ,(1974) , 10.1016/S0076-6879(74)34011-6
Dieter H. Wolf, Marion Hoffmann, Tryptophan Synthase from Yeast FEBS Journal. ,vol. 45, pp. 269- 276 ,(1974) , 10.1111/J.1432-1033.1974.TB03551.X
John C. Sheehan, George P. Hess, A New Method of Forming Peptide Bonds Journal of the American Chemical Society. ,vol. 77, pp. 1067- 1068 ,(1955) , 10.1021/JA01609A099
DAPHNE OWENS, CHRISTOPHER J. BAILEY, The Purification and Structure of Tryptophan Synthetase from Neurospora crassa Biochemical Society Transactions. ,vol. 2, pp. 1331- 1332 ,(1974) , 10.1042/BST0021331