Influence of acarbose and maltose on the reactivity of individual tryptophanyl residues in glucoamylase from aspergillus niger
Author:
Publisher
Springer Science and Business Media LLC
Subject
Biochemistry,General Medicine
Link
http://link.springer.com/content/pdf/10.1007/BF02907996.pdf
Reference46 articles.
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3. Beddell, C. R., C. C. F. Blake &S. J. Oatley: An X-ray study of the structure and binding properties of iodine-inactivated lysozyme. J. Mol. Biol. 97, 643–654 (1975)
4. Blake, C. C. F., R. Cassels, C. M. Dobson, F. M. Poulsen, R. J. P. Williams &K. S. Wilson: Structure and binding properties of hen lysozyme modified at tryptophan 62, J. Mol. Biol. 147, 73–95 (1981)
5. Boel, E., I., Hjort, B. Svensson, F. Norris, K. E. Norris &N. P. Fill: Glucoamylases G1 and G2 from Aspergillus niger are synthesized from two different but closely related mRNAs EMBO J. 3, 1097–1102 (1984)
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