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Active monopeptide prepared from active blood polypeptide and its prepn. activity and sequence

A technology of activity and separation process, applied in the field of active peptides and its preparation, can solve the problems of unseen separation and purification of active ingredients

Inactive Publication Date: 2005-06-22
NAT INST FOR THE CONTROL OF PHARMA & BIOLOGICAL PROD
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, since the deproteinized calf blood extract appeared on the market in 1955, most of its research has focused on its pharmacological effects and clinical applications, and there has been no report on the separation and purification of active ingredients from it.

Method used

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  • Active monopeptide prepared from active blood polypeptide and its prepn. activity and sequence
  • Active monopeptide prepared from active blood polypeptide and its prepn. activity and sequence
  • Active monopeptide prepared from active blood polypeptide and its prepn. activity and sequence

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0071] This example relates to the determination of the activity of isolated and purified samples using the Valscher respirometer manometry. details as follows:

[0072] Materials and instruments: Warburg respiration apparatus: Warburg system type 12062, produced by Braun-Melsungen, Germany; self-standardized reaction bottles without side arms; high-speed homogenizer; animals are clean-grade male guinea pigs with a weight of 250±10 g; four kinds of calves Blood deproteinized extracts are: Actovegin injection with batch number 152842 produced by Hafslund Nycomed AG in Austria; Socolseryl injection with batch number 414409 produced by Solco Basle in Switzerland; Cytopoietin with batch number 981216 produced by Jinzhou Medical College; The batch number 990102 of blood activity injection produced by Treasure Biopharmaceutical Co., Ltd. The reagents are: 10% KOH solution, 0.2mol / ml PBS and Brodie manometric fluid. The preparation method of calf blood deproteinized extract is as fo...

Embodiment 2

[0145] This embodiment relates to the determination of the molecular weight of Actovegin injection as a raw material for further separation and purification with high performance liquid gel chromatography (HPGC), specifically as follows:

[0146] Materials and instruments: High performance liquid chromatography: Beckman 125NM pump, 126NM detector, workstation; Superdex Peptide HR 10 / 300 column: 10mm×30cm, column volume 24ml, column packing particle size 22-44um, separation range 100-7000 channels Dayton, pressure value 1.5MPa, Pharmacia product; mobile phase: 0.05mol / L sodium phosphate+0.1mol / L sodium chloride aqueous solution, pH7.0.

[0147] The standard sample is: diribonuclease A with a relative molecular weight of 13700 Daltons, a Pharmacia product; insulin with a relative molecular weight of 5180 Daltons, a Fisherbrand product; somatostatin (14 peptides) with a relative molecular weight of 1508 Daltons; a relative molecular weight of 560 Dalton's hexapeptide, Biomol prod...

Embodiment 3

[0157] This embodiment relates to the high performance capillary zone electrophoresis (HPCZE) analysis of Actovegin injection.

[0158] Materials and instruments: Capillary electrophoresis apparatus: Beckman P / ACE 5000, fixed wavelength ultraviolet detector, workstation; Fused quartz capillary column: Beckman FS 75um * 57cm (effective length is 50cm); Sample Actovegin injection, batch number is the same as embodiment 1 ,2.

[0159] Method: prepare electrode buffer solution: take 1.7ml of 85% phosphoric acid, add 10ml of acetonitrile, add water to 250ml, 1mol / lNaOH, adjust the pH value to 2.5, filter with 0.45um membrane, and ultrasonicate before use. Before use, the capillary was washed with 1mol / l NaOH for 5 minutes, ultrapure water for 5 minutes, 0.1mol / l NaOH for 2 minutes, ultrapure water for 1 minute, and electrode buffer for 2 minutes before sample injection. The high-voltage sampling method is adopted, the sampling time is 3 seconds, the capillary sampling end is posit...

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Abstract

The invention discloses an active single peptide isolated from a calf blood deproteinized extract of active blood polypeptide, its preparation process, activity and sequence detection; the activity screening of each separated component is carried out by using the established activity determination method, And the biochemical properties were analyzed; using modern liquid chromatography method, after gel chromatography, C18 and C4 reverse phase chromatography, Silica and CN normal phase chromatography, the active ingredients in the protein-free extract of calf blood were separated and purified; Phase chromatography, high performance capillary electrophoresis, and mass spectrometry identified it as an active peptide and determined its molecular weight. The active peptide is mainly used for treating cerebrovascular diseases.

Description

Technical field: [0001] The invention discloses an active peptide and a preparation method thereof, in particular an active single peptide isolated from active blood polypeptide-calf blood deproteinized extract, a preparation method thereof, activity detection and sequence analysis and application of the active peptide. Background technique: [0002] Peptides are a class of biologically active substances. It involves many fields such as hormone, nerve cell growth and reproduction, and its importance lies in regulating the functional activities of various systems, organs and cells in the body. The study of bioactive peptides is one of the most active fields in current biological research. In the 1960s and 1970s, major breakthroughs were made in the separation and purification of some peptide hormones in the pituitary and hypothalamus. In the mid-1970s, the separation and purification of endogenous opioid peptides was successful, which greatly promoted the development of neur...

Claims

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Application Information

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IPC IPC(8): A61P9/10C07K1/16C07K5/00C07K19/00
Inventor 徐康森廖志湘
Owner NAT INST FOR THE CONTROL OF PHARMA & BIOLOGICAL PROD
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