Glycoprotein biosynthesis in the aortic wall. III. Study of soluble galagtosyl transferase in intimal cells

Enzyme inactivation kinetics typically follows what would appear to be simple first-order behavior. However, the inactivation process is known to involve a number of reversible (decomposition, denaturation) as well as irreversible (decomposition, aggregation, and coagulation) reactions. These reactions can combine to form a wide variety of reaction pathways which can potentially demonstrate complex inactivation kinetics. However, it was shown that with appropriate assumptions with regard to the relative magnitudes of the various reaction rates, many complex inactivation pathways can demonstrate apparent first-order behavior. Thus, with this analysis, a more accurate interpretation of the slope of an activity versus time semi-log plot can be obtained.

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Effect of subunit dissociation, denaturation, aggregation, coagulation, and decomposition on enzyme inactivation kinetics: I. First‐order behaviour

Lencki

Arul

Neufeld

1992

Biotech & Bioengineering

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Effect of subunit dissociation, denaturation, aggregation, coagulation, and decomposition on enzyme inactivation kinetics: II. Biphasic and grace period behavior

Lencki

Arul

Neufeld

1992

Biotech & Bioengineering

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A model previously developed to characterize enzymatic in activation behavior was used to explain the non-first-order biphasic and grace period phenomena that are often observed with oligomeric enzymes. Luciferase and urease were used as model enzyme such as luciferase, the oligomer initially dissociates reversibly into two native monomer species. These native monomers can then reversibly denature and irreversibly aggregate and coagulate. With the hexamer, urease, two trimers are formed that can subsequently aggregate to form an inactive hexamer. The dissociated monomer species of luciferase do not possess catalytic activity, so the inactivation mechanism, is biphasic; the first slope of a first-order kinetic plot is influenced by the reversible oligomer/monomer/denatured-monomer transition. Whereas the second slope is associated with either irreversible aggregation or coagulation. In contrast, the trimer of urease has the same activity as the hexamer; therefore, during the intitial hexamer-trimer transition, little activity loss occurs. However, as the trimer concentration increases, activity decreases as a result of trimer aggregation. As a result, grace period inactivation behavior is observed.

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Glycoprotein biosynthesis in splenic cells. Purification of a microsomal galactosyl-transferase

1976

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Glycoprotein biosynthesis in the aortic wall. III. Study of soluble galagtosyl transferase in intimal cells

Cited by 11 publications

References 27 publications

Effect of subunit dissociation, denaturation, aggregation, coagulation, and decomposition on enzyme inactivation kinetics: I. First‐order behaviour

Effect of subunit dissociation, denaturation, aggregation, coagulation, and decomposition on enzyme inactivation kinetics: I. First‐order behaviour

Effect of subunit dissociation, denaturation, aggregation, coagulation, and decomposition on enzyme inactivation kinetics: II. Biphasic and grace period behavior

Glycoprotein biosynthesis in splenic cells. Purification of a microsomal galactosyl-transferase

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