Changes of protein solutions during storage: a study of albumin pharmaceutical preparations

Biotechnology and Applied Biochemistry
Cathrine Christiansen, Tore Skotland

Abstract

During the production of air-filled albumin microspheres, to be used as an ultrasound contrast agent, it was observed that some albumin lots could not be used owing to albumin precipitation. In order to understand the reason for these lot-to-lot variations, 24 lots of 5% (w/v) human albumin pharmaceutical preparations were analysed. The results revealed that the good albumin lots all contained <0.03 mol of free SH groups per mol of albumin. The precipitation observed with other lots was most probably due to higher amounts of free SH groups. The lower amount of free SH groups in the good lots correlated with: (i) a yellow colour of the solutions and a UV-visible spectrum similar to that observed for non-enzymatic glycosylation; (ii) a decreased fructosamine content; (iii) an increased mobility against the anode in isoelectric focusing; and (iv) an increased truncation of the two N-terminal amino acids. No, or only small, differences were observed for the amounts of albumin dimer, albumin aggregates and protein impurities, and these could not account for the albumin precipitation. The differences observed between the albumin lots were most probably due to varying storage times and/or storage conditions, and incubation experiments...Continue Reading

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Citations

Apr 23, 2013·Fertility and Sterility·Phoebe H LeonardDean E Morbeck
Jun 19, 2013·Analytical Biochemistry·David Bar-OrLeonard T Rael
Dec 4, 2012·American Journal of Physiology. Heart and Circulatory Physiology·Jason CastleSteven B Feinstein

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