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Process for obtaining high efficiency human albumin for use in detoxification therapy

A technology for human albumin and albumin, which is applied in the field of obtaining high-capacity human albumin and can solve problems such as complicated processes

Active Publication Date: 2009-07-29
GRIFOLS
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

In the past, when heat treatment was not performed, special steps had to be included for the removal of PKA, which complicated the process

Method used

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  • Process for obtaining high efficiency human albumin for use in detoxification therapy
  • Process for obtaining high efficiency human albumin for use in detoxification therapy
  • Process for obtaining high efficiency human albumin for use in detoxification therapy

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0071] Example 1: Comparison of the effects of N-acetyltryptophan and sodium caprylate stabilizers on albumin binding capacity (ABiC)

[0072] In order to obtain albumin with a high binding capacity, it was decided to evaluate the extent to which sodium caprylate and N-acetyl tryptophan used to stabilize the commercial formulation affect the binding capacity of unstabilized albumin.

[0073] For this purpose, the ABiC is determined according to the established method, but with albumin without stabilizer as reference. Separate solutions of each excipient (N-acetyl tryptophan and octanoate) were prepared in increasing concentrations. 1 ml of each solution was incubated with 1 ml of albumin without stabilizer (final albumin concentration 1%). Then 1 ml of dansyl sarcosine was added to each mixture and the normal course was followed using the albumin binding volumetric method.

[0074] get the result in figure 1 It was shown that, for the same concentration of excipients, the a...

Embodiment 2

[0075] Example 2: Plasma Albumin Binding Capacity (ABiC) Stabilized with Different Commercially Available Albumin Concentrates and with N-Acetyl Tryptophan Prepared According to the Process Described in the Invention Without Stabilizers and with 0.16 mmol / g Compared with albumin, the results obtained in figure 2 show.

[0076] Taking the binding capacity (100%) shown by native plasma albumin (column A) as reference albumin, we observed The profile of binding capacity was all consistent (48% to 57%) between the different commercially available albumin concentrates of albumin (columns B to G) and compared with only sodium caprylate (0.099 mmol / g albumin) ( 52%) (column H) was consistent with commercially available albumin stabilized. This binding capacity is smaller than that of plasma albumin.

[0077] Albumin obtained according to the invention without stabilizer (127%) (column I) or stabilized at 0.16 mmol / g of N-acetyltryptophan ( 80%) (Column J) A higher binding capaci...

Embodiment 3

[0079] Example 3: Stability of albumin solutions. The albumin solution with a concentration of 20% obtained by the method described in the present invention is stabilized with 0.15M sodium chloride and a concentration of 0.16mmol N-acetyl tryptophanate / g albumin and in accordance with international level coordination , the current regulations on stability research Q5C "biotechnology / biological products" and Q1A (R2) "stability testing of new drugs, substances and products" conduct research on their stability. image 3 Stability at 20% albumin binding capacity is given. Real-time stability data for the 3 batches of albumin shown showed that the product remained stable. In particular, after at least 30 months of storage at 5°C±3°C and at 30°C±2°C, the binding capacity did not show appreciable changes from the beginning of the study. In fact the fluctuations in binding capacity results observed at 5°C and 30°C occurred in parallel with time and can therefore be attributed to ac...

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Abstract

Process for obtaining human albumin of high efficiency for use in detoxification therapy. The process comprises a) a first dialysis (diafiltration); b) the stabilisation of the solution with NaCl and at least one amino acid; c) heating the solution; d) a second dialysis (diafiltration).

Description

technical field [0001] The present invention relates to a method of obtaining human albumin with a high capacity for the transport of molecules such as in detoxification therapy or cell culture etc. or other applications. The present invention is based on the experimental use of purifying human albumin with high binding capacity and transport molecules and thereby enhancing the efficacy of detoxification treatments by removing toxins from the blood, preferably by albumin infusion, apheresis and by in vitro The system replaces albumin. Apheresis The method according to the invention consists in obtaining an albumin solution for therapeutic use in the inactivation of viruses, which has a high binding capacity, does not contain stabilizers, or contains specific stabilizers so that it maintains a high binding capacity. [0002] The essential nature of the invention is defined in claim 1 . [0003] Dependent claims 2 to 22 define further preferred aspects of the invention. Back...

Claims

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Application Information

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IPC IPC(8): C07K1/34C07K1/14C07K14/76A61K38/38A61P39/02
CPCA61K38/38C07K14/765A61P1/16A61P7/00A61P7/08A61P39/00A61P39/02A61P43/00
Inventor 胡安-伊格纳西奥·霍尔克拉-捏托皮尔·里斯托-德巴特蒙特塞拉特·科斯塔-里尔若拉
Owner GRIFOLS
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