scholarly journals The effect of low temperatures on enzyme activity

1995 ◽  
Vol 305 (1) ◽  
pp. 17-20 ◽  
Author(s):  
N More ◽  
R M Daniel ◽  
H H Petach
Keyword(s):  
Escherichia Coli ◽  
Enzyme Activity ◽  
Glutamate Dehydrogenase ◽  
Low Temperatures ◽  
Sharp Decrease ◽  
Bovine Liver ◽  
Extreme Thermophiles ◽  
Beta Glucosidase ◽  
The Stability ◽  
Beta Galactosidase

The stability of two enzymes from extreme thermophiles (glutamate dehydrogenase from Thermococcales strain AN1 and beta-glucosidase from Caldocellum saccharolyticum expressed in Escherichia coli) has been exploited to allow measurement of activity over a 175 degrees C temperature range, from +90 degrees C to -85 degrees C for the glutamate dehydrogenase and from +90 degrees C to -70 degrees C for the beta-glucosidase. The Arrhenius plots of these enzymes, and those for two mesophilic enzymes (glutamate dehydrogenase from bovine liver and beta-galactosidase from Escherichia coli), exhibit no downward deflection corresponding to the glass transition, found by biophysical measurements of several non-enzymic mesophilic proteins at about -65 degrees C and reflecting a sharp decrease in protein flexibility as the overall motion of groups of atoms ceases.

scholarly journals Properties of Antisera to Glutamate Dehydrogenase from Nitrogen-fixing Lupin Nodules

1985 ◽  
Vol 38 (1) ◽  
pp. 51 ◽  
Author(s):  
JR Kennedy ◽  
Z Wyszomirska-Dreher ◽  
Y T T chan ◽  
JW Chen
Keyword(s):  
Enzyme Activity ◽  
Glutamate Dehydrogenase ◽  
Bovine Liver ◽  
Lupinus Luteus ◽  
Plant Origin ◽  
Nitrogen Fixing ◽  
Leguminous Plants ◽  
Rhizobium Lupini

Antibody prepared in rabbit to lupin (Lupinus luteus) nodule glutamate dehydrogenase (GDH) crossreacted with all six isozymes of GDH isolated from lupin nodules. Rocket immunoelectrophoresis showed that the antisera were also strongly cross-reactive with GDH from other parts of the lupin plant and from the roots and stems of other leguminous plants and wheat, but not with GDH of Rhizobium lupini, lupin bacteroids or bovine liver. This confirms the exclusively plant origin of lupin nodule cytosolic GDH. Enzyme activity, determined spectrophotometrically, was strongly inhibited by the antibody. Substrates and modifiers of GDH did not influence the degree of this inhibition, indicating that the antiserum should be an effective reagent for study of the localization of GDH in plants.

Effect of the hydrophilicity of the polymer matrix on immobilized α-chymotrypsin

1984 ◽  
Vol 49 (6) ◽  
pp. 1552-1556
Author(s):  
Minoru Kumakura ◽  
Isso Kaetsu
Keyword(s):  
Thermal Stability ◽  
Enzyme Activity ◽  
Pore Size ◽  
Polymer Matrix ◽  
Low Temperatures ◽  
Radiation Polymerization ◽  
Thermal Stability Of

α-Chymotrypsin was immobilized by radiation polymerization at low temperatures and the effect of the hydrophilicity of the polymer matrix on the enzyme activity and thermal stability was studied. The activity and thermal stability of immobilized chymotrypsin increased with the increasing hydrophilicity of the polymer matrix or monomer. The thermal stability was affected by the form and pore size of the polymer matrix; chymotrypsin immobilized on a soft-gel polymer matrix exhibited an enhanced thermal stability.

scholarly journals Lysine and tyrosine in the NADH inhibitory site of bovine liver glutamate dehydrogenase.

1981 ◽  
Vol 256 (22) ◽  
pp. 11866-11872
Author(s):  
K.V. Saradambal ◽  
R.A. Bednar ◽  
R.F. Colman
Keyword(s):  
Glutamate Dehydrogenase ◽  
Bovine Liver ◽  
Inhibitory Site

scholarly journals The Stability of Acyl Carrier Protein in Escherichia coli

1973 ◽  
Vol 248 (12) ◽  
pp. 4461-4466
Author(s):  
Gary L. Powell ◽  
Michael Bauza ◽  
Allan R. Larrabee
Keyword(s):  
Escherichia Coli ◽  
Acyl Carrier Protein ◽  
Carrier Protein ◽  
The Stability

scholarly journals Sequence of Bovine Liver Glutamate Dehydrogenase

1971 ◽  
Vol 246 (8) ◽  
pp. 2374-2399 ◽  
Author(s):  
Michael Landon ◽  
Dennis Piszkiewicz ◽  
Emil L. Smith
Keyword(s):  
Glutamate Dehydrogenase ◽  
Bovine Liver
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