Review of methods for determination of total protein and peptide concentration in biological samples.

Clinical proteomics can be defined as the use of proteomic technologies to identify and measure biomarkers in fluids and tissues. The current work is intended to review various methods used for the determination of the total concentration of protein or peptide in fluids and tissues and the application of such methods to clinical proteomics. Specifically, this article considers the approaches to the measurement of total protein concentration, not the measurement of the concentration of a specific protein or group of proteins in a larger mixture of proteins.

Identifying residues in antigenic determinants by chemical modification.

Chemical modification of the side chains of amino acid residues was one of the first methods developed to investigate epitopes in protein antigens. The principle of the method is that alteration of the structure of a key residue of an epitope by a chemical modification will alter reactivity with antibody by affecting either specificity or avidity or both. Chemical modification has the advantage that it can be applied to discontinuous as well as continuous epitopes and may be of value in identifying cryptic epitopes.

Considerations Regarding the Use of Blood Samples in the Proteomic Identification of Biomarkers for Cancer Diagnosis.

Blood is the most common source of biomarkers for use in the diagnosis and prognosis of malignant disease. Utilizing proteomic technology for biomarker identification offers greatly increased sensitivity. Such an increase in sensitivity requires precise sample preparation to eliminate any bias in analysis.

The interaction of thrombin with blood platelets.

Thrombin is a potent agonist of platelets. In the current article, the research on the interaction of thrombin with blood platelets is reviewed starting with the first studies demonstrating the direct action of thrombin on platelets and ending with an analysis of the importance of the protease-activated receptors (PARs) and the GpIb complex. The antithrombin activity of platelets is discussed in terms of the binding of thrombin to receptor(s) on the platelet surface.

A review of the therapeutic uses of thrombin.

Thrombin is the product of the hemostatic response essential to the conversion of fibrinogen to fibrin. In addition, it is also responsible for the aggregation of blood platelets in the formation of the "platelet plug" as well as the activation of factor VIII, factor V, factor XI, factor XIII and protein C. The action of thrombin is not confined to the hemostatic response as it also has a critical function in the wound healing process by stimulating 'mitogenic' events through interaction with cell surface receptors.

A critical review of the methods for cleavage of fusion proteins with thrombin and factor Xa.

Expression and purification of proteins in recombinant DNA systems is a powerful and widely used technique. Frequently there is the need to express the protein of interest as a fusion protein or chimeric protein. Fusion protein technology is frequently used to attach a "signal" which can be used for subsequent localization of the protein or a "carrier" which can be used to deliver a "therapeutic" such as a radioactive molecule to a specific site.

An adventure in biotechnology: the development of haemophilia A therapeutics -- from whole-blood transfusion to recombinant DNA to gene therapy.

The past decade has seen an explosion in the number of therapeutic proteins available for a wide spectrum of diseases. Some of these proteins are obtained from human plasma. Examples of these therapeutic proteins are albumin, intravenous immunoglobulins and prothrombin complex concentrates.