Properties and stabilization of an extracellular α-glucosidase from the extremely thermophilic archaebacteria Thermococcus strain AN 1: enzyme activity at 130°C-Reference-Cited by-同舟云学术

Properties and stabilization of an extracellular α-glucosidase from the extremely thermophilic archaebacteria Thermococcus strain AN 1: enzyme activity at 130°C

Published:1996-01 Issue:1 Volume:1292 Page:197-205
ISSN:0167-4838
Container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

Author:

Piller Karin,Daniel Roy M.,Petach Helen H.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Structural Biology

Reference27 articles.

1. A cell-associated oligo-1,6-α-glucosidase from an extremely thermophilic anaerobic bacterium, Thermoanaerobium Tok6-B1

2. Glutamate dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus

3. Glutamate dehydrogenase from the extremely thermophilic archaebacterial isolate AN1

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