Protein modifications during antiviral heat bioprocessing and subsequent storage

Biotechnology Progress

Volumn 17, Issue 5, 2001, Pages 974-978

  Smales, C M ^a   Pepper, D S ^a   James, D C ^a  

^a UNIVERSITY OF KENT   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIVIRAL HEAT TREATMENT; BIOPROCESSING;

BIOPROCESS; EGG WHITE; HEAT TREATMENT; HEN; LYSOZYME; PROTEIN ENGINEERING; PROTEIN MODIFICATION; PROTEIN STABILITY; QUALITY CONTROL; SUCROSE; VIRUS PROTEIN;

HEAT TREATMENT; OXIDATION; SUGAR (SUCROSE);

PROTEINS;

ANIMALS; CHICKENS; DRUG STABILITY; DRUG STORAGE; EGG PROTEINS; GLYCOLYSIS; GLYCOSYLATION END PRODUCTS, ADVANCED; HEAT; MURAMIDASE; PROTEINS; SPECTROMETRY, FLUORESCENCE; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; STERILIZATION; SUCROSE;

EID: 0034799235     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1021/bp010086f     Document Type: Article

References (9)

1. Current status of viral safety of virus inactivated factor VIII and IX concentrates in treatment of hemophilia
2. Factor VIII inhibitors in previously treated haemophilia A patients with a double virus-inactivated plasma-derived factor VIII concentrate
3. Protein modification during antiviral heat bioprocessing
4. Mechanisms of protein modification during model anti-viral heat-treatment bioprocessing of β-lactoglobulin variant A in the presence of sucrose
5. The clinical significance of glycation
6. A systematic approach to evaluate the modification of lens proteins by glycation-induced cross-linking
7. Immunochemical detection of advanced glycosylation end products in vivo
8. Rapid formation of advanced glycation end-products by intermediate metabolites of glycolytic pathway and polyol pathway