Premium
Synthesis and immunological evaluation of an eicosapeptide related to the C‐terminus of the β‐subunit of human chorionic gonadotropin
Author(s) -
Schneider C.H.,
Blaser K.,
Pfeuti Ch.,
Gruden E.
Publication year - 1975
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(75)80506-0
Subject(s) - clinical immunology , citation , chemistry , psychology , medicine , library science , immunology , computer science , allergy
Human chorionic gonadotropin (HCG) is a glycoprotein hormone which is composed of two dissimilar subunits. The a-subunit seems to occur in closely similar form in a number of glycoproteins including LH, FSH and TSH, whereas the P-subunit contains homologous as well as specific structural regions. Sequence studies by the group of Bahl [l] and Canfield [2] showed that the P-subunit contains a C-terminal sequence of 30 amino acids which does not occur in hLH and appears to represent a relatively extended unique structure exclusively occurring in the chorionic gonadotropin molecule. This feature may be of immediate practical interest provided that the C-terminal chain is sufficiently accessible within the structure of the entire hormone to allow interaction with antibodies raised against an adequate portion of the unique sequence. We here describe the synthesis of an eicosapeptide related to the C-terminus of the &subunit of HCG and