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Tissue‐specific molecular heterogeneity of human growth hormone‐releasing hormone receptor protein
Author(s) -
Fujinaka Yuichi,
Yokogoshi Yutaka,
Zhang Chen-Yu,
Okura Toshihiro,
Kitagawa Kouki,
Saito Shiro
Publication year - 1996
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(96)00917-9
Subject(s) - receptor , antibody , biology , peptide , hormone receptor , thyrotropin releasing hormone receptor , chemistry , microbiology and biotechnology , biochemistry , immunology , genetics , cancer , breast cancer
A site‐directed anti‐peptide antibody (anti‐hGHRHRc18) was generated against the cytoplasmic tail of human GHRH receptor. The dissociation constant ( K d ) and the antibody binding site (AbT) of anti‐hGHRHRc18 were 2.5 nmol/l and 0.54 nmol/l, respectively. In an immunoblotting experiment, affinity‐purified anti‐hGHRHRc18 specifically recognized a single 50‐kDa protein in human pituitary. In a screening of the expression of GHRH receptor protein in extra‐pituitary tissues, only human kidney showed a single 52‐kDa protein. Our results suggest that the GHRH receptor protein exhibits tissue‐specific molecular heterogeneity.