Chemical modification of carboxyl groups in glucoamylase from Aspergillus niger-Reference-Cited by-同舟云学术

Chemical modification of carboxyl groups in glucoamylase from Aspergillus niger

Published:1988-01 Issue:6 Volume:53 Page:331-342
ISSN:0105-1938
Container-title:Carlsberg Research Communications
language:en
Short-container-title:Carlsberg Res. Commun.

Author:

Svensson Birte,Møller Hanne,Clarke Anthony J.

Publisher

Springer Science and Business Media LLC

Subject

Biochemistry,General Medicine

Link

http://link.springer.com/content/pdf/10.1007/BF02983309.pdf

Reference61 articles.

1. Ananthanarayanan, V.S. &C.C. Bigelow: Unusual difference spectra of proteins containing tryptophan. I. Studies with model compounds. Biochemistry 8, 3717–3723 (1969)

2. Ananthanarayanan, V.S. &C.C. Bigelow: Unusual difference spectra of proteins containing tryptophan. II. Studies with proteins. Biochemistry 8, 3723–3728 (1969)

3. Ariki, M. &T. Fukui: Modification of rabbit muscle phosphorylase b by a water-soluble carbodiimide. J. Biochem. 83, 183–190 (1978)

4. Ashikari, T., N. Nakamura, Y. Tanaka, N. Kiuchi, Y. Shibano, T. Tanaka, T. Amachi &H. Yoshizumi: Rhizopus raw-starch-degrading glucoamylase: its cloning and expression in yeast. Agric. Biol. Chem. 50, 957–964 (1986)

5. Blake, C.C.F., L.N. Johnson, G.A. Mair, A.C.T. North, D.C. Phillips &V.R. Sarma: Crystallographic studies of the activity of hen egg-white lysozyme. Proc. Roy. Soc. SerB 167, 378–387 (1967)

Cited by 13 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Carboxyl groups and tryptophan residues in the active site ofRhizopus niveus glucoamylase;Journal of Basic Microbiology;1999-12

2. Chemical modification of xylanase from Trichosporon cutaneum shows the presence of carboxyl groups and cysteine residues essential for enzyme activity;Journal of Protein Chemistry;1999

3. Efficient purification, characterization and partial amino acid sequencing of two α-1,4-glucan lyases from fungi;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1997-05

4. Functional roles and subsite locations of Leu177, Trp178 and Asn182 of Aspergillus awamori glucoamylase determined by site-directed mutagenesis;"Protein Engineering, Design and Selection";1993

5. 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;Carbohydrate Research;1992-04