Unlock instant, AI-driven research and patent intelligence for your innovation.

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: 2013-05-29
GRIFOLS
View PDF7 Cites 0 Cited by
  • 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

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
  • 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

[0072] Example 1: Comparison of the effects of N-acetyltryptophan and sodium caprylate stabilizers on albumin binding capacity (ABiC)

[0073] In order to obtain albumin with high binding capacity, it was decided to evaluate the extent to which sodium caprylate and N-acetyltryptophan used to stabilize the commercially available formulations affect the unstabilized albumin binding capacity.

[0074] For this reason, ABiC was determined according to the set method, but albumin without stabilizer was used as the benchmark. Separate solutions of each excipient (N-acetyltryptophan and caprylate) were prepared in increasing concentrations. Incubate 1 ml of each solution with 1 ml of albumin without stabilizer (final albumin concentration of 1%). Then 1 ml of dansyl sarcosine was added to each mixture and the normal course was followed using the albumin binding capacity measurement method.

[0075] The result is in figure 1 It shows that for the same concentration of excipients, the albu...

Embodiment 2

[0076] Example 2: Plasma albumin binding capacity (ABiC) is compared with different commercially available albumin concentrates and prepared according to the method described in the present invention without stabilizers and with 0.16mmol / g of N-acetyltryptophan stabilized Comparison of albumin, the results obtained are in figure 2 display.

[0077] Taking the binding capacity (100%) shown by natural plasma albumin (column A) as the benchmark albumin, we observed that the concentration of N-acetyltryptophan and sodium caprylate with stabilizer is 0.064 to 0.096mmol / g In the different commercial albumin concentrates between albumin, the binding capacity is all the same (48% to 57%) (columns B to G) and compared with only sodium caprylate (0.099mmol / g albumin) ( 52%) (Column H) The stable commercial albumin is consistent. The binding capacity is less than the binding capacity of plasma albumin.

[0078] Based on the comparison with the commercially available concentrated solution o...

Embodiment 3

[0080] Example 3: Stability of albumin solution. The 20% albumin solution obtained by the method described in the present invention is stabilized with 0.15M sodium chloride and a concentration of 0.16mmol N-acetyltryptophan salt / g albumin and is coordinated with the international level , The current regulations on stability research Q5C "Biotechnology / Biological Products" and Q1A (R2) "Stability Testing of New Drugs, Substances and Products", research their stability. image 3 The stability of the 20% albumin binding capacity is given. The real-time stability data of the three batches of albumin shown show that the product remains stable. In particular, after storage at 5°C±3°C and at 30°C±2°C for at least 30 months, the binding capacity did not show appreciable changes from the beginning of the study. In fact, the fluctuations in the binding capacity results observed at 5°C and 30°C occur in parallel with time, and are therefore attributable to the actual variability of the t...

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

Process for obtaining high-potency human albumin for use in detoxification therapy. The method comprises a) a first dialysis (diafiltration); b) stabilization of the solution by means of NaCl and at least one amino acid; c) heating of the solution; d) a second dialysis (diafiltration).

Description

Technical field [0001] The present invention relates to a method for obtaining human albumin with high capacity, which is used to transport molecules, for example, in detoxification therapy or cell culture or other applications. The present invention is based on experiments to purify human albumin with high binding capacity and transport molecules and thereby improve the efficacy of detoxification treatment by removing toxins in the blood, preferably through albumin injection, plasma apheresis and through vitro The system replaces albumin. Plasma apheresis according to the present invention includes obtaining an albumin solution that is used for virus inactivation therapy and has a high binding capacity, does not contain a stabilizer, or contains a specific stabilizer to maintain a high binding capacity. [0002] The basic properties of the present invention are defined in claim 1. [0003] The dependent claims 2 to 22 define other preferred aspects of the invention. Background t...

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 Patents(China)
IPC IPC(8): C07K1/34C07K1/14C07K14/76A61K38/38A61P39/02
CPCA61K38/38C07K14/765A61P1/16A61P39/00A61P39/02A61P43/00A61P7/00A61P7/08
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
Features
  • R&D
  • Intellectual Property
  • Life Sciences
  • Materials
  • Tech Scout
Why Patsnap Eureka
  • Unparalleled Data Quality
  • Higher Quality Content
  • 60% Fewer Hallucinations
Social media
Patsnap Eureka Blog
Learn More

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

© 2025 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap|About US| Contact US: help@patsnap.com