Effect of excipients on the stability and structure of lyophilized recombinant human growth hormone

Journal of Pharmaceutical Sciences

Volumn 87, Issue 11, 1998, Pages 1412-1420

  Costantino, Henry R ^a   Carrasquillo, Karen G ^a   Cordero, Rocio A ^a   Mumenthaler, Marco ^a   Hsu, Chung C ^a   Griebenow, Kai ^a  

^a GENENTECH INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA METHYL MANNOSIDE; CELLOBIOSE; EXCIPIENT; HUMAN GROWTH HORMONE; LACTOSE; MANNITOL; SORBITOL; TREHALOSE;

ALPHA HELIX; BINDING SITE; CONFERENCE PAPER; CRYSTALLIZATION; DRUG FORMULATION; DRUG STABILITY; DRUG STRUCTURE; INFRARED SPECTROSCOPY; LYOPHILISATE; PROTEIN AGGREGATION; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; X RAY POWDER DIFFRACTION;

EID: 0031734413     PISSN: 00223549     EISSN: None     Source Type: Journal    
DOI: 10.1021/js980069t     Document Type: Conference Paper

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48. Only the a-helix content is a good indicator for structural conservation in the co-lyophilizates, because the /3-sheet content is inflated by the formation of intermolecular /(-sheets. Such intermolecular /8-sheets can simply be a result of protein-protein contacts caused by the removal of the solvent water.