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Human Thrombin (human + thrombin)

Distribution by Scientific Domains
Medical Sciences40%

Selected Abstracts

Protein Detecting Arrays Based on Cationic Polythiophene,DNA-Aptamer Complexes,

ADVANCED MATERIALS, Issue 20 2006
Abérem, M. Béra
By combining an appropriate DNA aptamer with a cationic polythiophene optical transducer, human thrombin can be specifically detected on microarrays in the attomole range in less than one hour without any tagging of the target. The system can be modified and utilized as a probe for the detection of various proteins or other biomolecules. This work opens new interesting possibilities for simple and rapid multiparametric analysis in genomics and proteomics. [source]

Review article: recent advances in the management of bleeding gastric varices

ALIMENTARY PHARMACOLOGY & THERAPEUTICS, Issue 1 2006
D. TRIPATHI
Summary Gastric variceal bleeding can be challenging to the clinician. Tissue adhesives can control acute bleeding in over 80%, with rebleeding rates of 20,30%, and should be first-line therapy where available. Endoscopic ultrasound can assist in better eradication of varices. The potential risks of damage to equipment and embolic phenomena can be minimized with careful attention to technique. Variceal band ligation is an alternative to tissue adhesives for the management of acute bleeding, but not for secondary prevention due to a higher rate of rebleeding. Endoscopic therapy with human thrombin appears promising, with initial haemostasis rates typically over 90%. The lack of controlled studies for thrombin prevents universal recommendation outside of clinical trials. Balloon occluded retrograde transvenous obliteration is a recent technique for patients with gastrorenal shunts, although its use is limited to clinical trials. Transjugular intrahepatic portosystemic stent shunt is an option for refractory bleeding and secondary prophylaxis, with uncontrolled studies demonstrating initial haemostasis obtained in over 90%, and rebleeding rates of 15,30%. Non-cardioselective , -blockers are an alternative to transjugular intrahepatic portosystemic stent shunt for secondary prophylaxis, although the evidence is limited. Shunt surgery should be considered in well-compensated patients. Splenectomy or embolization is an option in patients with segmental portal hypertension. [source]

Ultrastructure of activated mouse platelets: A qualitative scanning electron microscopy study

MICROSCOPY RESEARCH AND TECHNIQUE, Issue 6 2008
E. Pretorius
Abstract Platelets form an integral part of the coagulation process, and their ultrastructure can provide valuable information regarding diseases associated with hemostasis. During coagulation, platelets aggregate; this aggregation can be achieved in vitro, by adding thrombin to platelet-rich plasma. Previous research showed that human thrombin could be used successfully to activate mouse platelets. When conservative changes are included, the amino acid similarity between human and mouse thrombin is ,75%. In this qualitative study, we compare the ultrastructure of mouse platelet aggregates activated by human thrombin as well as two concentrations of mouse thrombin, using the scanning electron microscope. Results show that both human and mouse thrombin activate platelets to form aggregates with typical pseudopodia formation. Magnification up to 250,000× showed membrane morphology with the open canalicular system pores visible in both the mouse- and human-activated platelets. It is therefore concluded that mouse platelets can be successfully aggregated using either mouse or human thrombin. Microsc. Res. Tech. 2008. © 2008 Wiley-Liss, Inc. [source]

Epitope mapping of a monoclonal antibody against human thrombin by H/D-exchange mass spectrometry reveals selection of a diverse sequence in a highly conserved protein

PROTEIN SCIENCE, Issue 6 2002
Abel Baerga-Ortiz
Abstract The epitope of a monoclonal antibody raised against human thrombin has been determined by hydrogen/deuterium exchange coupled to MALDI mass spectrometry. The antibody epitope was identified as the surface of thrombin that retained deuterium in the presence of the monoclonal antibody compared to control experiments in its absence. Covalent attachment of the antibody to protein G beads and efficient elution of the antigen after deuterium exchange afforded the analysis of all possible epitopes in a single MALDI mass spectrum. The epitope, which was discontinuous, consisting of two peptides close to anion-binding exosite I, was readily identified. The epitope overlapped with, but was not identical to, the thrombomodulin binding site, consistent with inhibition studies. The antibody bound specifically to human thrombin and not to murine or bovine thrombin, although these proteins share 86% identity with the human protein. Interestingly, the epitope turned out to be the more structured of two surface regions in which higher sequence variation between the three species is seen. [source]