enzyme assay

An example progress curve for an enzyme assay is shown above.

To address these deficiencies, other techniques using enzyme assay have been developed.

Both carrier and prenatal testing using enzyme assay became available in the 1970s.

All the enzyme assays were run in triplicate.

All lysosomal enzyme assays were linear with respect to time and protein concentration.

Different mutations have different effects on enzyme assay results.

The ligand binding or enzyme assay data suggesting a potential for the adverse effects.

All enzyme assays measure either the consumption of substrate or production of product over time.

Enzyme assays are used to screen for galactosemia and biotinidase deficiency.

Blood serum is often used for enzyme assay testing because it can be sampled inexpensively.

Enzyme assays are laboratory methods for measuring enzymatic activity.

Enzyme assays are laboratory procedures that measure the rate of enzyme reactions.

Because serum can be drawn at low cost and without an invasive procedure, it is the preferred tissue for enzyme assay testing.

In enzyme assay, success with one targeted population cannot always be generalized to other populations, because the mutation base is diverse.

The majority of patients are initially screened by enzyme assay, which is the most efficient method to arrive at a definitive diagnosis.

Numerous methods of enzyme assays are available to quantitatively follow enzyme reactions.

Enzyme assays are commonly done using fluorometric detection or radioactively labeled substrates.

The Zymoblot technique is simpler, cheaper, more reliable and less time consuming than all known procedures for enzyme assays.

These tests include clinical examination, biopsy, genetic testing, molecular analysis of cells or tissues, and enzyme assays.

Enzyme assay indicates the effectiveness of a given enzyme to a specific substrate and serves as a quality control tool.

Because of pseudodeficiency alleles, the results of enzyme assay testing in one population cannot be generalized to other populations.

To measure the initial (and maximal) rate, enzyme assays are typically carried out while the reaction has progressed only a few percent towards total completion.

The enzyme assay may be invalid because of differences between the natural substrate and an artificial substrate used in testing.

The focus was on a simple tripeptide Phe-Ala-Pro, which in earlier enzyme assays has shown inhibition activity.

For example, in the enzyme assay discussed above, a standard curve may be produced by making many different samples with different quantities of the enzyme.