期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1978
卷号：75
期号：11
页码：5516-5519
DOI：10.1073/pnas.75.11.5516
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：The amino acid sequence of blastokinin, also called uteroglobin, has been determined by a combined study of both the intact native molecule and the peptide fragments resulting from tryptic and chymotryptic digestions. Sequence analyses performed by automated methods and by sequential digestion with leucine aminopeptidase and carboxypeptidase Y demonstrate that blastokinin is a dimer of identical 69-amino acid subunits held together in parallel orientation by two disulfide bridges at positions 3 and 68. The polypeptide chains are further characterized by the absence of tryptophan residues and by single residues of histidine and tyrosine at positions 8 and 21, respectively. Six of eight amino acids, positions 17--24, near the progesterone binding site of blastokinin contain a hydroxyl group. Knowledge of the chemistry of this receptor site should allow better perspectives of the chemistry of molecules in normal tissues that are dependent on progesterone for growth and development, as well as compounds that could act as cancer antagonists for endocrine therapy of hormone-dependent tumors.
