ISSN: 2155-9872

Revista de técnicas analíticas y bioanalíticas

Acceso abierto

Nuestro grupo organiza más de 3000 Series de conferencias Eventos cada año en EE. UU., Europa y América. Asia con el apoyo de 1.000 sociedades científicas más y publica más de 700 Acceso abierto Revistas que contienen más de 50.000 personalidades eminentes, científicos de renombre como miembros del consejo editorial.

Revistas de acceso abierto que ganan más lectores y citas
700 revistas y 15 000 000 de lectores Cada revista obtiene más de 25 000 lectores

Indexado en
  • Índice de fuentes CAS (CASSI)
  • Índice Copérnico
  • Google Académico
  • sherpa romeo
  • Base de datos de revistas académicas
  • Abrir puerta J
  • Revista GenámicaBuscar
  • TOC de revistas
  • InvestigaciónBiblia
  • Infraestructura Nacional del Conocimiento de China (CNKI)
  • Directorio de publicaciones periódicas de Ulrich
  • Biblioteca de revistas electrónicas
  • Búsqueda de referencia
  • Directorio de indexación de revistas de investigación (DRJI)
  • Universidad Hamdard
  • EBSCO AZ
  • OCLC-WorldCat
  • director académico
  • Catálogo en línea SWB
  • Biblioteca Virtual de Biología (vifabio)
  • publones
  • Pub Europeo
  • ICMJE
Comparte esta página

Abstracto

Utilizing Enzymatic Method, Fibrin-Zymography and Liquid Chromatography Mass Spectrometry to Identify the Active Protein in Lumbrokinase Drug Substance

Hong Jiang

Lumbrokinase, extracted from the cultured earthworm of Eisenia fetida, is widely used to prevent or treat thrombosis as biochemical medicine in China. However, the molecular mechanism and protein components in the drug have not been clearly understood and the specification could not illustrate its characteristic comprehensively. In this study, we investigated the mechanism of lumbrokinase by the fibrin plate method. The results revealed that all the five manufacturers’ products contained both fibrinolytic components and kinase components. We used the method of fibrinzymography to show the existence and activity of lumbrokinase. The fibrin-zymography showed that lumbrokinase was a group of fibrinolytic proteins and there were slight differences between the products of different manufacturers. Besides, we proved the fibrin-zymogram gel could be used as the identification method to distinguish Eisenia fetida from other earthworm species. Then we identified the ingredients by mass spectrometry. The results suggested that fibrinolytic related components existed in the drug, including fifteen proteins. We further compared these proteins with other serine proteins. We observed the amino acid sequence and the catalytic triad of the identified proteins were similar with human trypsin and bovine trypsin. Besides, some also had similar characteristics with human tissue-type (tPA) plasminogen activators and urokinase (uPA) plasminogen activators. These results demonstrated lumbrokinase products contained two major groups of protein components, which suggested two different functions. One is the direct degradation of fibrin; the other is indirectly dissolving thrombus by activating the plasminogen into plasmin.

Descargo de responsabilidad: este resumen se tradujo utilizando herramientas de inteligencia artificial y aún no ha sido revisado ni verificado.