A homogeneous chemiluminescent immunoassay method.

A new homogeneous chemiluminescent immunoassay method featuring the use of specific binding members separately labeled with an acridan-based chemiluminescent compound and a peroxidase is reported. Formation of an immunocomplex brings the chemiluminescent compound and the peroxidase into close proximity. Without any separation steps, a chemiluminescent signal is generated upon addition of a trigger solution, and the intensity is directly correlated to the quantity of the analyte.

Characterization of new fluorescent peroxidase substrates.

The reagents Lumigen PS-1 and Lumigen PS-3 were originally developed as chemiluminescent substrates for ultrasensitive detection of horseradish peroxidase (HRP) in homogeneous solution and membrane blotting assays. However, an additional unique feature of these acridan-based reagents is the generation of a fluorescent species on reaction with peroxidase, a property which has been termed as chemifluorescence. These reagents, therefore, represent the first dual-use substrates enabling both chemiluminescent and fluorescent detection.

The C-S lyases of higher plants: homogeneous beta-cystathionase of spinach leaves.

S-Substituted cysteines and their derivatives are prominent secondary amino acids in a number of plant families. The substituents are often specific and unique to each family. Cystathionine, however, is an ubiquitous S-substituted cysteine found in all autotrophic plants since it is an intermediate in the biosynthesis of methionine.

The C-S Lyases of Higher Plants : Direct Comparison of the Physical Properties of Homogeneous Alliin Lyase of Garlic (Allium sativum) and Onion (Allium cepa).

Garlic and onion alliin lyases, although from closely related species, have many differences. The two enzymes differ in their K(m) values, pH optima, and isoelectric points. There is a major difference in their molecular weight and subunit structure.

The C-S lyases of higher plants: preparation and properties of homogeneous alliin lyase from garlic (Allium sativum).

Alliin lyase from garlic (Allium sativum) has been purified to homogeneity. The purification procedure involves the use of affinity chromatography on concanavalin A-Sepharose 4B. Addition of polyvinylpolypyrrolidone to the homogenizing medium greatly improves the specific activity of the extract.