Semisynthetic engineering of proteinase inhibitor homologues.
Biochim Biophys Acta
; 913(1): 97-101, 1987 May 27.
Article
en En
| MEDLINE
| ID: mdl-2437960
ABSTRACT
A semisynthetic approach to modulate the inhibitory specificity of aprotinin, the Kunitz trypsin inhibitor from bovine mast cells, is described. By the use of peptide-chemical procedures a single amino acid of its reactive site can be replaced by any other coded or non-coded amino acid. Thus, a series of aprotinin homologues have been prepared which demonstrate the individual contribution of a single side chain to the inhibition of a particular target proteinase and enable specific inhibitors to be designed.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Aprotinina
Idioma:
En
Revista:
Biochim Biophys Acta
Año:
1987
Tipo del documento:
Article