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Evidence that progesterone binding uteroglobin is similar to myosin alkali light chain
Author(s) -
Baker Michael E.
Publication year - 1985
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(85)81021-8
Subject(s) - uteroglobin , myosin , calmodulin , chemistry , trifluoperazine , calcium , calcium binding protein , biophysics , endocrinology , biology , biochemistry , gene , organic chemistry
Using a computer program designed to detect evolutionary relationships between proteins, I find that exon 2 of rabbit uteroglobin, a progesterone binder, and part of myosin alkali light chain have a comparison score that is 7.2 standard deviations higher than that obtained with a comparison of randomized sequences of these proteins. The probability ( p ) of getting this score by chance is less than 10 −12 . This theoretical finding that these sequences are similar has led to the experimental finding that copper, calcium and the tranquilizer trifluoperazine, a calmodulin binding ligand, affect progesterone binding to uteroglobin.