Looking for breakthrough ideas for innovation challenges? Try Patsnap Eureka!

Application of recombination FN polypeptide in preparing medicine for treating severe infectious diseases such as septicemia

A technique for severe infection, sepsis, applied in the field of medicine

Inactive Publication Date: 2008-02-13
FUJIAN MEDICAL UNIV UNION HOSPITAL
View PDF0 Cites 2 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

The application of the heparin-binding domain polypeptide in the molecular structure of FN to study its effect on mouse sepsis and DIC models has not been reported at home and abroad

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Application of recombination FN polypeptide in preparing medicine for treating severe infectious diseases such as septicemia
  • Application of recombination FN polypeptide in preparing medicine for treating severe infectious diseases such as septicemia
  • Application of recombination FN polypeptide in preparing medicine for treating severe infectious diseases such as septicemia

Examples

Experimental program
Comparison scheme
Effect test

Embodiment Construction

[0092] The present invention is described in detail below in conjunction with accompanying drawing and embodiment:

[0093] 1. Construction of recombinant FN heparin-binding domain polypeptide yeast expression vector and preparation of polypeptide

[0094] In the present invention, the heparin-binding domain polypeptide gene at the FNC end and the heparin-binding domain polypeptide gene at the FNN end are cloned into a yeast expression vector, and expressed in GS115 yeast cells.

[0095] 1.1) Design of primers for PCR amplification of the heparin-binding domain polypeptide gene at the FNC end and the FNN end

[0096] According to the FN cDNA sequence and the comparison with the amino acid sequence in the molecular structure of FN, the cloning positions of the fibronectin C-terminal heparin-binding domain polypeptide (rhFNHC-36) and the N-terminal heparin-binding domain polypeptide (rhFNHN-29) were determined, and yeast The enzyme cutting site of the expression vector, the PCR...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

PUM

PropertyMeasurementUnit
molecular weightaaaaaaaaaa
molecular weightaaaaaaaaaa
molecular weightaaaaaaaaaa
Login to View More

Abstract

The invention discloses an N-terminal heparin binding domain polypeptide and a C-terminal binding domain polypeptide of a recombinant fibronectin. The N-terminal heparin binding domain polypeptide consists of five I-type homologous structures of the N-terminal of a FN molecule, including 237 aminophenols, which are from Ser46 to Gly282. A DNA sequence which codes the polypeptide is from 403bp to 1113bp with a length of 711bp. A FCR amplified fragment length is 741bp; a fragment length after double digestion is 729bp. A polypeptide molecular weight, which is expressed by barm, is 28.52kDa. The C-terminal heparin binding domain polypeptide consists of three III-type homologous structures of the FN molecule, including 272 aminophenols, which are from Tyr1720 to Tyr1991. The DNA sequence which codes the polypeptide is from 5428bp to 6244bp with a length of 816bp. The FCR amplified fragment length is 835bp; the fragment length after double digestion is 828bp. The polypeptide molecular weight, which is expressed by barm, is 36.09kDa. The invention is applied to medicine preparations for a serious infection of septicemia, a hemorrhage of thrombocytopenia and a disseminated intravascular coagulation.

Description

Technical field: [0001] The invention relates to the field of medicine, in particular to the preparation of recombinant FN heparin binding domain polypeptide and its application in medicines for severe infection such as sepsis, thrombocytopenia bleeding and disseminated intravascular coagulation. Background technique: [0002] Fibronectin, fibronectin, hereinafter referred to as FN; recombinant fibronectin N-terminal heparin-binding domain polypeptide, containing 237 amino acids, molecular weight 29kDa, referred to as rhFNHN-29, recombinant fibronectin C-terminal heparin-binding domain polypeptide, containing 272 amino acids , with a molecular weight of 36kDa, referred to as rhFNHC-36; fibronectin heparin-binding domain I, namely the fibronectin N-terminal heparin-binding domain, referred to as HepI; fibronectin heparin-binding domain II, namely the fibronectin C-terminal heparin-binding domain, referred to as HepII; disseminated intravascular coagulation, Disseminated Intra...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

Application Information

Patent Timeline
no application Login to View More
Patent Type & Authority Applications(China)
IPC IPC(8): A61K38/14A61P31/04A61P7/04A61P7/02
Inventor 陈元仲邹起练吴勇郭江睿陈小芳
Owner FUJIAN MEDICAL UNIV UNION HOSPITAL
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Patsnap Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Patsnap Eureka Blog
Learn More
PatSnap group products