Synthesis of 31- and 35-amino acid carboxyl terminal fragments of the .beta. subunit of the human chorionic gonadotropin

1977 ◽  
Vol 42 (21) ◽  
pp. 3341-3343 ◽  
Author(s):  
George H. Fisher ◽  
Ding Chang ◽  
Geralidine Howard ◽  
Karl Folkers
Keyword(s):  
Amino Acid ◽  
Chorionic Gonadotropin ◽  
Human Chorionic Gonadotropin ◽  
Beta Subunit ◽  
Carboxyl Terminal

scholarly journals Recognition of the Beta-subunit of human chorionic gonadotropin and sub-determinants by target tissue receptors

1978 ◽  
Vol 176 (2) ◽  
pp. 599-602 ◽  
Author(s):  
S Ramakrishnan ◽  
C Das ◽  
G P Talwar
Keyword(s):  
Amino Acid ◽  
Chorionic Gonadotropin ◽  
Human Chorionic Gonadotropin ◽  
Leydig Cells ◽  
Beta Subunit ◽  
Peptide Sequence ◽  
Target Tissue ◽  
Amino Acid Residues ◽  
Testosterone Production ◽  
Tissue Receptors

The beta-subunit of human chorionic gonadotropin, purified immunochemically to eliminate undissociated human chorionic gonadotropin, induced testosterone production by mouse Leydig cells at concentrations 400-fold higher than human chorionic gonadotropin. Steroidogenesis was also stimulated by a synthetic fragment of the beta-subunit of human chorionic gonadotropin conforming to the peptide sequence residues 39–71, whereas peptide sequence residues 39–56 and three C-terminal fragments (residues 115–145, 111–145 and 101–145) failed to cause steroidogenesis. These studies suggest the presence in the beta-subunit of human chorionic gonadotropin of determinants recognized by the tissue receptors, a part of these determinants residing between amino acid residues 57–71.

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