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Titolo:
Evaluation of protein modification during anti-viral heat bioprocessing byelectrospray ionization mass spectrometry
Autore:
Smales, CM; Pepper, DS; James, DC;
Indirizzi:
Univ Kent, Res Sch Biosci, Canterbury CT2 7NJ, Kent, England Univ Kent Canterbury Kent England CT2 7NJ nterbury CT2 7NJ, Kent, England Scottish Natl Blood Transfus Serv, Edinburgh EH1 1EY, Midlothian, ScotlandScottish Natl Blood Transfus Serv Edinburgh Midlothian Scotland EH1 1EY d
Titolo Testata:
RAPID COMMUNICATIONS IN MASS SPECTROMETRY
fascicolo: 5, volume: 15, anno: 2001,
pagine: 351 - 356
SICI:
0951-4198(2001)15:5<351:EOPMDA>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
FACTOR-VIII CONCENTRATE; HEMOPHILIA-A PATIENTS; INACTIVATED FACTOR-VIII; GLYCATION END-PRODUCTS; IN-VITRO GLYCATION; MAILLARD-REACTION; VIRUS INACTIVATION; AMADORI; SAFETY; N-EPSILON-(CARBOXYMETHYL)LYSINE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Smales, CM Univ Kent, Res Sch Biosci, Canterbury CT2 7NJ, Kent, England Univ Kent Canterbury Kent England CT2 7NJ 2 7NJ, Kent, England
Citazione:
C.M. Smales et al., "Evaluation of protein modification during anti-viral heat bioprocessing byelectrospray ionization mass spectrometry", RAP C MASS, 15(5), 2001, pp. 351-356

Abstract

During the preparation of therapeutic plasma and recombinant protein biopharmaceuticals heat-treatment is routinely applied as a means of viral inactivation. However, as most proteins denature and aggregate under heat stress, it is necessary to add thermostabilizing excipients to protein formulations destined for anti-viral heat-treatment in order to prevent protein damage. Anti-viral heat-treatment bioprocessing therefore requires that a balance be found between the bioprocessing conditions, virus kill and protein integrity. In this study we have utilized a simple model protein, beta -lactoglobulin, to investigate the relationship between virucidal heat-treatment conditions (protein formulation and temperature) and the type and extent of protein modification in the liquid state. A variety of industrially relevant heat-treatments were undertaken, using formulations that included sucroseas a thermostabilizing excipient. Using liquid chromatography/electrosprayionization mass spectrometry (LC/ESI-MS) we show here that protein mo difications do occur with increasingly harsh heat-treatment. The predominant modification under these conditions was protein glycation by either glucose or fructose derived from hydrolyzed sucrose. Advanced glycation end productsand additional unidentified products were also present in beta -lactoglobulin protein samples subjected to extended heat-treatment. These findings have implications for the improvement of anti-viral heat-treatment bioprocesses to ensure the safety and efficacy of protein biopharmaceuticals. Copyright (C) 2001 John Wiley & Sons, Ltd.

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Documento generato il 04/07/20 alle ore 15:02:28