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

Application of tachyplesin in preparing antihrombotic medicines and health-care products and preparation method thereof

The technology of an antithrombotic drug and a limulus peptide is applied to the application of the limulus peptide in the preparation of antithrombotic drugs and health care products and the field of preparation thereof, and can solve the problem of not finding the limulus peptide and the like.

Inactive Publication Date: 2011-09-21
GUANGDONG MEDICAL UNIV
View PDF1 Cites 9 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

After searching, it was found that there is currently no literature reporting the antithrombotic function of the limulus peptide, and there is no report on the use of the limulus peptide derived from Limulus blood cells as an antithrombotic drug or health care product 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 tachyplesin in preparing antihrombotic medicines and health-care products and preparation method thereof
  • Application of tachyplesin in preparing antihrombotic medicines and health-care products and preparation method thereof
  • Application of tachyplesin in preparing antihrombotic medicines and health-care products and preparation method thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0052] The lysate of Limulus hemocytes prepares the process steps of Limulus peptide as follows:

[0053] (1) Extract fresh Limulus blood with sterile non-pyrogenic equipment, centrifuge at 1000 rpm for 5 minutes, lyse the cells with 20 mmol / L HCl, break up the sticky cell clumps with a homogenizer, and obtain the crude extract.

[0054] (2) The crude liquid was centrifuged at 8000 rpm for 15 minutes, and the supernatant was collected.

[0055](3) Filter the supernatant with three layers of gauze, separate it with dextran G-50 (Sephadex G-50) (1.5cm×90cm), and elute with 20mmol / L HCl solution at a flow rate of 1.0mL / min. There are three groups of peaks, and the eluted product of the third group is collected, the solution is adjusted to pH 6.0-7.0, centrifuged at 10,000 rpm for 15 minutes, and the supernatant is freeze-dried and stored. It was confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) that it was a single electrophoresis band with a mole...

Embodiment 2

[0057] The process steps of preparing limulus peptide from the remaining waste in the production of Limulus reagent are as follows:

[0058] (1) Collect the cell lysate aggregates produced during the production of LAL, add 20mmol / L HCl solution, and use a homogenizer to break up the sticky cell aggregates to obtain the crude extract.

[0059] (2) The crude liquid was centrifuged at 8000 rpm for 15 minutes, and the supernatant was collected.

[0060] (3) Filter the supernatant with three layers of gauze, separate it with dextran G-50 (Sephadex G-50) (1.5cm×90cm), and elute with 20mmol / L HCl solution at a flow rate of 1.0mL / min. There are three groups of peaks, and the eluted product of the third group is collected, the solution is adjusted to pH 6.0-7.0, centrifuged at 10,000 rpm for 15 minutes, and the supernatant is freeze-dried and stored. It was confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) that it was a single electrophoresis band with ...

Embodiment 3

[0062] The process steps for preparing limulus peptide from unqualified limulus reagent raw materials are as follows:

[0063] (1) Add 20mmol / L HCl solution to the unqualified Limulus reagent raw material, and adjust the pH value of the solution to 3.

[0064] (2) The crude liquid was centrifuged at 8000 rpm for 15 minutes, and the supernatant was collected.

[0065] (3) Filter the supernatant with three layers of gauze, separate it with dextran G-50 (Sephadex G-50) (1.5cm×90cm), and elute with 20mmol / L HCl solution at a flow rate of 1.0mL / min. There are three groups of peaks, and the eluted product of the third group is collected, the solution is adjusted to pH 6.0-7.0, centrifuged at 10,000 rpm for 15 minutes, and the supernatant is freeze-dried and stored. It was confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) that it was a single electrophoresis band with a molecular weight of about 2KDa.

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

No PUM Login to View More

Abstract

The invention belongs to an application of tachyplesin in preparing antihrombotic medicines and healthcare products and a preparation method thereof. Tachyplesin is applied in preparing antiplatelet aggregation and antihrombotic medicines and healthcare products as a component of antiplatelet aggregation and antihrombotic medicines and healthcare products, or as a precursor of antiplatelet aggregation and antihrombotic medicines. Prepared from production wastes of horseshoe crab hemocytes or horseshoe crab reagents, such tachyplesin is capable of obviously inhibiting platelet aggregation and preventing thrombosis; and the tachyplesin has excellent antiplatelet aggregation performance and prolongs bleeding time (BT) and clotting time (CT).

Description

technical field [0001] The invention belongs to the application of tachyplesin peptide (tachyplesin) in the preparation of antithrombotic drugs and health care products and a preparation method thereof. Background technique [0002] Thrombotic disease is a common disease, often manifested as myocardial infarction, ischemic cerebral infarction, and venous thromboembolism. Every year, 1 to 3 people per 1,000 people suffer from different forms of thrombotic disease, which is a kind of disease that seriously affects health. At present, the clinical drugs for the treatment of thrombotic diseases are mainly divided into antiplatelet drugs, anticoagulant drugs and thrombolytic drugs. [0003] Antiplatelet drugs can inhibit the adhesion, aggregation and release of platelets, thereby preventing thrombus formation. Antiplatelet drugs can effectively prevent the occurrence of cardiovascular diseases and prolong the survival period of patients. Antiplatelet drugs are increasingly wide...

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
IPC IPC(8): A61K38/10C07K7/08C07K1/16A61P7/02
Inventor 张海涛刘文
Owner GUANGDONG MEDICAL UNIV
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