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Preparations stabilized over long time

A preparation and stable technology, applied in the field of G-CSF preparations, can solve problems such as contamination, complex virus removal, deterioration, etc.

Inactive Publication Date: 2006-12-20
CHUGAI PHARMA CO LTD
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, adding this protein stabilizer also brings some problems, such as the necessary and very complicated process of removing viral contamination
[0009] However, in the absence of this protein, Met (methionine)-oxidized G-CSF may be produced again, which poses the problem of spoilage

Method used

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  • Preparations stabilized over long time
  • Preparations stabilized over long time
  • Preparations stabilized over long time

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0093] The effect of pH value on the remaining rate of G-CSF

[0094] Calculate the residual rate of G-CSF in samples 1 and 2 prepared according to different pH values ​​in Table 1 after the accelerated test at 60°C for 2 weeks and 50°C for 1 month according to the equation in method 1. The results are shown in Table 3.

[0095] Sample 1, pH7.4

[0096] As shown in the table, the formulation at pH 6.5 is more stable than that at pH 7.4.

Embodiment 2

[0098] Effects of Various Amino Acids on G-CSF Surplus Rate (1)

[0099] Prepare samples 3-6 (containing G-CSF 100 μg) and samples 7-10 (containing G-CSF 250 μg) according to the amino acids listed in Table 1, and calculate according to the equation in method 1. Accelerated test at 60°C for 2 weeks and 50°C for 1 month The remaining rate of G-CSF in the above preparations. The results are shown in Tables 4 and 5.

[0100] Sample 3

[0101] Sample 7

[0102] The addition of phenylalanine or arginine alone improved stability at any G-CSF content compared to formulations without amino acids, but not significantly. Adding phenylalanine and arginine at the same time can significantly improve the stability of the preparation.

Embodiment 3

[0104] Effects of Various Amino Acids on G-CSF Surplus Rate (2)

[0105] According to the amino acids listed in Table 1, prepare samples 11-20 (containing phenylalanine as amino acid 1, and lysine, histidine, arginine, aspartic acid, glutamic acid, serine, threonine , tyrosine, asparagine and glutamine as amino acid 2), and samples 21-33 (containing arginine as amino acid 1, and alanine, valine, leucine, isoleucine acid, methionine, tryptophan, phenylalanine, proline, glycine, serine, threonine, asparagine and glutamine as the amino acid 2), calculated according to the equation in method 160 The residual rate of G-CSF in the above preparations after 2 weeks at ℃ and 1 month at 50℃. The results are shown in Tables 6 and 7.

[0106] 50℃, January

[0107] 50℃, January

[0108] It can be observed that phenylalanine and lysine, phenylalanine and histidine, phenylalanine and arginine, phenylalanine and aspartic acid, phenylalanine and gluta...

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PUM

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Abstract

A stable G-CSF formulation containing one or more amino acids selected from the group consisting of lysine, histidine, arginine, aspartic acid, glutamic acid, threonine and asparagine; one or more amino acids selected from hydrophobic amino acids; and methionine. A method for inhibiting the formation of the methionine residue-oxidized derivative of a physiologically active protein having methionine residues characterized by adding methionine to a composition containing this protein.

Description

[0001] The present invention is a divisional application of the Chinese patent application submitted on February 29, 2000 with the application number 00804421.X and the title of the invention "long-term stable preparation". technical field [0002] The present invention relates to G-CSF (Granulocyte Colony Stimulating Factor) preparations, in particular to particularly stable G-CSF preparations with little loss of active ingredient and low methionine-oxidized G-CSF content. Background technique [0003] G-CSF is a glycoprotein with a molecular weight of about 20,000, which acts on the precursor cells of neutrophils to promote their proliferation and differentiation to mature. [0004] High-purity human G-CSF can be purified by culturing a tumor cell line from a patient with oral basal carcinoma. At present, human G-CSF gene has been successfully cloned by genetic engineering technology, and recombinant human G-CSF can be mass-produced from metamorphosis or animal cells. We ...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): A61K38/14A61K47/16A61K47/26A61K9/19A61P37/04A61K9/00A61K31/195A61K31/198A61K38/00A61K38/18A61K38/19A61K38/29A61K47/18C12N5/07C12N5/071
CPCA61K47/183A61K9/0019A61K9/19A61K31/195A61K31/198A61K38/1816A61K38/193A61K38/29A61K47/26A61K47/20A61P37/04A61K2300/00A61K47/18
Inventor 佐藤泰
Owner CHUGAI PHARMA CO LTD
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