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The preparation and properties of hornblende as a support for immobilized invertase
The suitability of hornblende as a support for immobilized β‐fructofuranosidase (invertase) was studied, with regard to the physical stability of the support and the thermal and operational stability… Expand
Studies on the stability of immobilized xanthine oxidase and urate oxidase
The stability of immobilized preparations of xanthine oxidase and urate oxidase was studied, and optimized, because of the potential joint use of both enzymes in clinical analysis. Xanthine oxidase… Expand
Some factors affecting the stability of glucoamylase immobilized on hornblende and on other inorganic supports
Glucoamylase from four different companies was studied: three had similar stability (half‐life at 50°C about 140 hr); the fourth was less stable (half‐life at 50°C about 20 hr). The immobilized… Expand
Urate oxidase immobilization on elastin.
Observations on the effect of bicarbonate on the stability of horse liver alcohol dehydrogenase
Abstract 1. 1. Horse liver alcohol dehydrogenase was less stable in Tris/HCO−3 buffer (half-life at 30°C was 40 hr) than in Tris/Cr buffer (half-life at 30°C was 130hr). 2. 2. Bicarbonate did not… Expand
Preliminary investigations on the immobilization of yeast alcohol dehydrogenase
Studies on yeast alcohol dehydrogenase bound to solid supports.
The stability of bound enzyme was enhanced by increasing the quantity of protein bound: coimmobilized albumin had a stabilizing effect and depended on support or linkage method as follows. Expand
Yeast alcohol dehydrogenase immobilized on sepharose derivatives by non-specific adsorption followed by cross-linkage with glutaraldehyde.
- S. Barry, T. Griffin, Desmond B. Johnson
- Chemistry, Medicine
- The International journal of biochemistry
Alcohol dehydrogenase was adsorbed on acetyl and phenylglycyl derivatives of agarose and albumin co-immobilized with the enzyme increased its stability above that of soluble enzyme. Expand
Inhibitors of adenosine diphosphate ribosyl transferase suppress the induction of ornithine decarboxylase
Some observations on the effects of glutaraldehyde on horse liver alcohol dehydrogenase
- Desmond B. Johnson
Abstract 1. 1. Commercial glutaraldehyde behaved as a substrate for horse liver alcohol dehydrogenase (HL-ADH) in the direction NADH → NAD. The K m for glutaraldehyde was 0.006% (w/v) in phosphate… Expand