Immunoglobulin G (IGG) concentrate depleted of anti-A and anti-B antibodies and of polyreactive IGGS

A technology of immunoglobulin, polyreactivity, applied in the field of obtaining the above-mentioned concentrate, capable of solving problems such as adverse side effects

Active Publication Date: 2009-01-14
分馏和生物工艺法国实验室公司
View PDF9 Cites 6 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

As a result, administered levels of polyreactive IgG produced by IgG concentrate production methods can lead to adverse side effects such as fever, nausea, or headache

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
  • Immunoglobulin G (IGG) concentrate depleted of anti-A and anti-B antibodies and of polyreactive IGGS
  • Immunoglobulin G (IGG) concentrate depleted of anti-A and anti-B antibodies and of polyreactive IGGS
  • Immunoglobulin G (IGG) concentrate depleted of anti-A and anti-B antibodies and of polyreactive IGGS

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0132] A sample of IgG concentrate (B2) at 40 g / l was obtained following the method described in WO 02 / 092632.

[0133] A chromatographic column with a length of 50 cm and a diameter of 44 mm was loaded with a 50 / 50 (v / v) GLYCOSORB ABO medium mixture, which was grafted with trisaccharides equivalent to blood type A and blood type B epitopes, and then pre- Rinse it with 1200ml of water.

[0134] Inject the B2IgG concentrate at a rate of 0.21 / ml medium with the pump. Once the contents have permeated the cylinder, the cylinder is flushed with a minimum volume of injectable ready water (IP) to collect the IgG present in the column dead volume.

[0135] Antibody A and Antibody B and polyreactive IgG were removed from which a B3IgG concentrate of about 40 g / l was collected, then ultrafiltration was used to obtain a concentrate of 60 g / l, viruses were removed by nanofiltration on three series of filters, and Decreasing limits of persistence are obtained at 100, 50 and 20nm.

[013...

Embodiment 2

[0137] Example 2: Quantitative analysis of anti-A / Bs in IgIVs

[0138] 1) Test principle

[0139] 1-1) Preparation of human red blood cells

[0140] Normalize human erythrocyte suspensions of A Rhesus+, B Rhesus+, or O Rhesus+ blood type to 40 × 10 6 Concentration of erythrocytes / ml in PBS buffer at pH=7.4+1% BSA.

[0141] 1-2) Prepare the monoclonal D antibody range

[0142] A monoclonal D antibody (designated R297) was prepared for detection of absorbance (OD) at 280 nm relative to PBS buffer at pH 7.4. Relative to the composition in different amino acids, the molar extinction coefficient (ε) of the protein was calculated, and the concentration of monoclonal anti-D was obtained by the following formula:

[0143] C=OD / E1, where 1 is equal to the width of the container used for OD determination.

[0144] A monoclonal anti-D antibody ranging from 0 to 200 ng / ml was produced at 12 points (200; 150; 100; 75; 50; 25; 12.5; 6.25; 3.13; 1.56; 0.78 and Ong / ml).

[0145] 1-3) ...

Embodiment 3

[0175] A 1% (v / v) suspension of erythrocytes in blood group A was prepared in PBS buffer, pH 7.4, containing 1 wt.% bovine serum albumin (BSA). 50 μl of erythrocyte suspension was taken out and added to a flow cytometry tube (Beckmann-Coulter Epics XL)) and 50 μl of internal standard solution to measure the flow rate. The suspension is calibrated to 40.10 6 RBC / ml.

[0176] Eight IgG solutions were prepared by serially diluting the IgG concentrate (v / v) (B3) obtained from Example 1 by a factor of 2, with a maximum concentration of 30 g / l and a maximum dilution of 0.234 g / l . Then, a volume of 50 μl of the suspension was put into each well of a 96-well microplate, and then 50 μl of IgG solutions of different dilutions were added.

[0177] The whole solution was incubated at 37°C for 2 hours with stirring.

[0178] Each well was washed with 200 μl of PBS buffer including the aforementioned BSA, and the microplate was centrifuged at 2000 rpm for 1 minute. After clearing the ...

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
lengthaaaaaaaaaa
widthaaaaaaaaaa
Login to view more

Abstract

The present invention relates to an immunoglobulin G concentrate for therapeutic use, in which the respective contents of anti-A and anti-B antibodies are in accordance with a negative result in the in vitro indirect Coombs test. This IgG concentrate also has a polyreactive IgG content of between 0.01% and 0.1%, in particular between 0.07% and 0.1%, relative to the total content of IgG.

Description

technical field [0001] The present invention relates to an immunoglobulin G (IgG) concentrate depleted of anti-A (AcaA) and anti-B (AcaB) antibodies, with significantly reduced polyreactivity, and to a process for obtaining said concentrate. Background technique [0002] Since Cohn developed the ethanol precipitation method, human plasma enriched with immunoglobulin (Ig) components has been used for the treatment of various infections or congenital defects (Cohn et al., 1946, J.Am.Chem.Soc.68, 459; Oncley et al., 1949, J. Am Chem. Soc. 71, 541). [0003] There is an increasing need for highly purified Ig complex structures for intravenous injection (IgIV), eg obtained from human plasma. The complex structure of immunoglobulins (tetrapeptide chains linked by disulfide bonds), as well as the various antibodies present in the plasma mixture from thousands of blood donors, are currently unable to promote the development of immunoglobulin biotechnology. factor. Although monocl...

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): A61K39/395A61P43/00C07K16/00C07K1/36
CPCC07K16/00C07K16/34A61P31/00A61P31/04A61P37/00A61P43/00A61K39/395C07K1/36
Inventor 阿布德萨塔·什图鲁弗雷德里克·戴诺菲利普·保兰托纳奇
Owner 分馏和生物工艺法国实验室公司
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Try Eureka
PatSnap group products

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap