isozyme

Isozyme abundance has also been shown to be tissue specific.

Each isozyme responds slightly differently to each of these factors.

A mitochondrial isozyme of the encoded protein also has been characterized.

The second isozyme may be found in the absence of other urea cycle enzymes.

Xylulose, contained in red blood cells, is composed of both a major and minor isozyme.

For those diagnosed with essential Pentosuria, the major isozyme appears to be the same as the minor one.

Amiodarone inhibits the action of the cytochrome P450 isozyme family.

The latter exists as an isozyme located in both the mitochondrion and the cytosol.

By 1982 Goheen had confirmed that they were similar but not identical, probably by isozyme analysis.

Isozyme 3 is responsible for 17-beta-hydroxysteroid dehydrogenase deficiency.

The first isozyme, pancreatic elastase 1 was initially thought to be expressed in the pancreas.

The isozymes differ radically in their regulation and the discussions above are based on liver isozyme.

Deficiency in the liver isozyme leads to argininemia, which is usually associated with hyperammonemia.

It codes for an isozyme of pyruvate dehydrogenase kinase.

Specifically, the HK1 isozyme is involved.

Each isozyme is encoded by a separate gene:

The mitochondrial isozyme seems to be the most biologically important of these three, since mice lacking this enzyme die soon after birth.

It has four diagnostic isozyme loci.

A 1988 isozyme study showed very high rates of outcrossing; pollen from one plant is well-mixed among other plants in the locale.

The unique azoreductase isozyme from Bacillus sp.

Isozyme 2 is localized in the mitochondrial intermembrane space and may play a role in apoptosis.

Plants express a variety of cytosolic isozymes as well as what seems to be a chloroplast isozyme.

It is an inhibitor of cytochrome P450 2D6 and may interfere with other drugs metabolized by this isozyme.

Isoenzyme and isozyme are homologous proteins.

The activity of human CTPS1 isozyme has been demonstrated to be inhibited by phosphorylation.