Properties and stabilization of an extracellular α-glucosidase from the extremely thermophilic archaebacteria Thermococcus strain AN 1: enzyme activity at 130°C
- 4 January 1996
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1292 (1), 197-205
- https://doi.org/10.1016/0167-4838(95)00203-0
Abstract
No abstract availableKeywords
This publication has 18 references indexed in Scilit:
- Glutamate dehydrogenase from the extremely thermophilic archaebacterial isolate AN1Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1993
- New carbohydrate-based materials for the stabilization of proteinsJournal of the American Chemical Society, 1992
- Enzyme thermoinactivation in anhydrous organic solventsBiotechnology & Bioengineering, 1991
- Glutamate dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricusEuropean Journal of Biochemistry, 1991
- Enzyme immobilization via monoclonal antibodies I. Preparation of a highly active immobilized carboxypeptidase ABiotechnology & Bioengineering, 1986
- A new procedure for the synthesis of polyethylene glycol-protein adducts; Effects on function, receptor recognition, and clearance of superoxide dismutase, lactoferrin, and α2-macroglobulinAnalytical Biochemistry, 1983
- Enzyme stabilization by immobilizationAnalytical Biochemistry, 1979
- Three forms of .ALPHA.-glucosidase and a glucoamylase from Aspergillus awamori.Agricultural and Biological Chemistry, 1977
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Immobilized enzymes: The catalytic properties of lactate dehydrogenase covalently attached to glass beadsBiochemical and Biophysical Research Communications, 1973