Svensson B - Search Results

1

Thermodynamics of inhibitor binding to the catalytic site of glucoamylase from Aspergillus niger determined by displacement titration calorimetry.

Sigurskjold BW, Berland CR, Svensson B. Sigurskjold BW, et al. Among authors: svensson b. Biochemistry. 1994 Aug 23;33(33):10191-9. doi: 10.1021/bi00199a048. Biochemistry. 1994. PMID: 8060985

2

Kinetic identification of a hydrogen bonding pair in the glucoamylase-maltose transition state complex.

Sierks MR, Svensson B. Sierks MR, et al. Among authors: svensson b. Protein Eng. 1992 Mar;5(2):185-8. doi: 10.1093/protein/5.2.185. Protein Eng. 1992. PMID: 1350675

Earlier studies of mutant Glu180----Gln GA had indicated a role in substrate binding for Glu180 (Sierks, M.R., Ford, C., Reilly, P.J. and Svensson, B. (1990) Protein Engng, 3, 193-198). Here, changes in activation energies calculated from measured kcat/Km values for …

Earlier studies of mutant Glu180----Gln GA had indicated a role in substrate binding for Glu180 (Sierks, M.R., Ford, C., Reilly, P.J. and …

3

Primary structure of barwin: a barley seed protein closely related to the C-terminal domain of proteins encoded by wound-induced plant genes.

Svensson B, Svendsen I, Højrup P, Roepstorff P, Ludvigsen S, Poulsen FM. Svensson B, et al. Biochemistry. 1992 Sep 22;31(37):8767-70. doi: 10.1021/bi00152a012. Biochemistry. 1992. PMID: 1390663

4

Sierks MR, Bock K, Refn S, Svensson B. Sierks MR, et al. Among authors: svensson b. Biochemistry. 1992 Sep 22;31(37):8972-7. doi: 10.1021/bi00152a038. Biochemistry. 1992. PMID: 1390684

5

Stopped-flow fluorescence and steady-state kinetic studies of ligand-binding reactions of glucoamylase from Aspergillus niger.

Olsen K, Svensson B, Christensen U. Olsen K, et al. Among authors: svensson b. Eur J Biochem. 1992 Oct 15;209(2):777-84. doi: 10.1111/j.1432-1033.1992.tb17348.x. Eur J Biochem. 1992. PMID: 1425682 Free article.

6

Roles of the aromatic side chains in the binding of substrates, inhibitors, and cyclomalto-oligosaccharides to the glucoamylase from Aspergillus niger probed by perturbation difference spectroscopy, chemical modification, and mutagenesis.

Svensson B, Sierks MR. Svensson B, et al. Carbohydr Res. 1992 Apr 6;227:29-44. doi: 10.1016/0008-6215(92)85059-9. Carbohydr Res. 1992. PMID: 1499029

7

Identification of carboxylic acid residues in glucoamylase G2 from Aspergillus niger that participate in catalysis and substrate binding.

Svensson B, Clarke AJ, Svendsen I, Møller H. Svensson B, et al. Eur J Biochem. 1990 Feb 22;188(1):29-38. doi: 10.1111/j.1432-1033.1990.tb15367.x. Eur J Biochem. 1990. PMID: 2108020 Free article.

8

Side chain reactivities of glucoamylase G2 from Aspergillus niger evaluated by group-specific chemical modifications.

Håkansson K, Svensson B. Håkansson K, et al. Among authors: svensson b. Carlsberg Res Commun. 1989;54(4):145-56. doi: 10.1007/BF02907184. Carlsberg Res Commun. 1989. PMID: 2516722

9

Characterization of a glucoamylase G2 from Aspergillus niger.

Svensson B, Larsen K, Gunnarsson A. Svensson B, et al. Eur J Biochem. 1986 Feb 3;154(3):497-502. doi: 10.1111/j.1432-1033.1986.tb09425.x. Eur J Biochem. 1986. PMID: 3081341 Free article.

10

Structural studies on the O-glycosidically linked carbohydrate chains of glucoamylase G1 from Aspergillus niger.

Gunnarsson A, Svensson B, Nilsson B, Svensson S. Gunnarsson A, et al. Among authors: svensson s, svensson b. Eur J Biochem. 1984 Dec 17;145(3):463-7. doi: 10.1111/j.1432-1033.1984.tb08578.x. Eur J Biochem. 1984. PMID: 6439561 Free article.

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