Ramakrishnan S, Das C, Talwar G P
Biochem J. 1978 Nov 15;176(2):599-602. doi: 10.1042/bj1760599.
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.
人绒毛膜促性腺激素的β亚基经免疫化学纯化以去除未解离的人绒毛膜促性腺激素,它在比人绒毛膜促性腺激素高400倍的浓度下可诱导小鼠睾丸间质细胞产生睾酮。符合肽序列残基39 - 71的人绒毛膜促性腺激素β亚基的合成片段也能刺激类固醇生成,而肽序列残基39 - 56以及三个C末端片段(残基115 - 145、111 - 145和101 - 145)未能引起类固醇生成。这些研究表明人绒毛膜促性腺激素的β亚基中存在被组织受体识别的决定簇,其中一部分决定簇位于氨基酸残基57 - 71之间。