Immunoreactivity and receptor binding of mixed recombinants of human growth hormone and chorionic somatomammotropin.

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Abstract
The behavior in 6 radioligand assays of the recombinant obtained by the noncovalent complementation of the reduced and carbamoylmethylated 134-residue amino-terminal fragment of human growth hormone with the reduced and carbamoylmethylated 51-residue carboxyl-terminal fragment of human chorionic somatomammotropin was compared to that of the analogous recombinant of the 133-residue amino-terminal fragment of human chorionic somatomammotropin and the 51-residue carboxyl-terminal fragment of human growth hormone. The determinants for the hepatic growth hormone receptor binding and for the lactogenic receptor binding of human growth hormone are on the amino-terminal fragments. The antigenic determinants for a monospecific antiserum to human growth hormone and a monospecific antiserum to human chorionic somatomammotropin also are on the amino-terminal fragments of their respective antigens. The mixed recombinant of the amino-terminal fragment of human growth hormone with the carboxyl-terminal fragment of human chorionic somatomammotropin retains full radioimmuno- and radioreceptor activity after lyophilization.