Studies on the reduction and reoxidation of the disulfide bonds of the alpha and beta subunits of human choriogonadotropin.
Biochim Biophys Acta
; 533(1): 140-6, 1978 Mar 28.
Article
em En
| MEDLINE
| ID: mdl-638185
ABSTRACT
Reoxidation of the disulfide bonds of the alpha-subunit of human choriogonadotropin after their complete reduction yields a product which is indistinguishable from the native subunit in its electrophoretic pattern in polyacrylamide gel and in its ability to recombine with the beta subunit of bovine lutropin. The circular dichroism of reoxidized human choriogonadotropin-alpha is essentially identical to that of the native alpha-subunit, except for slightly more negative ellipticity in the region of 240 mm. Hybrid hormone preparations obtained by recombination of reoxidized or native human choriogonadotropin-alpha with native lutropin-beta exhibit identical electrophoretic patterns in polyacrylamide gels, elution profiles in gel filtration, receptor binding activities, and CD spectra. However, reoxidation of human choriogonadotropin-beta under the same conditions does not yield a product which resembles the native beta subunit in its electrophoretic pattern on gels, its CD spectrum or its ability to recombine with the alpha subunit.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Gonadotropina Coriônica
Limite:
Humans
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
1978
Tipo de documento:
Article