New approaches for high-yield purification of Müllerian inhibiting substance improve its bioactivity.
J Chromatogr B Analyt Technol Biomed Life Sci
; 766(1): 89-98, 2002 Jan 05.
Article
en En
| MEDLINE
| ID: mdl-11820299
ABSTRACT
We have established a new method to purify Müllerian inhibiting substance (MIS) with higher purity and recovery over existing procedures. Recombinant human MIS was expressed in Chinese hamster ovary cells and secreted into chemically defined serum-free media. The secreted products were concentrated by either precipitation with ammonium sulfate or lectin-affinity chromatography, each of which was followed by anion-exchange chromatography. Further separation of the active carboxy-terminal domain of MIS was achieved after cleavage by plasmin followed by lectin-affinity chromatography. This method may be applicable to other members of the transforming growth factor beta family with which MIS shares sequence homology.
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Banco de datos:
MEDLINE
Asunto principal:
Hormonas Testiculares
/
Glicoproteínas
/
Inhibidores de Crecimiento
Límite:
Animals
/
Humans
Idioma:
En
Revista:
J Chromatogr B Analyt Technol Biomed Life Sci
Asunto de la revista:
ENGENHARIA BIOMEDICA
Año:
2002
Tipo del documento:
Article
País de afiliación:
Estados Unidos