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
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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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