Structural similarity of bovine lung prostaglandin F synthase to lens epsilon-crystallin of the European common frog.

摘要: Abstract Cloned cDNA sequences specific for prostaglandin F (PGF) synthase have been isolated from a library of bovine lung mRNA sequences. Nucleotide-sequence analyses cloned inserts revealed that PGF consists 969-base pair open reading frame coding 323-amino acid polypeptide with Mr 36,666. The sequence analysis indicates shows 62% identical plus conservative substitutions compared human liver aldehyde reductase [Wermuth, B., Omar, A., Forster, Francesco, C., Wolf, M., Wartburg, J.P., Bullock, B. & Gabbay, K.H. (1987) in Enzymology and Molecular Biology Carbonyl Metabolism: Aldehyde Dehydrogenase, Aldo-Keto Reductase, Alcohol eds. Weiner, H. Flynn, T.G. (Liss, New York), pp. 297-307], which is similar to molecular weight substrate specificity. However, comparison the amino National Biomedical Research Foundation protein data base reveals 225 acids C termini epsilon-crystallin European common frog (Rana temporaria) [Tomarev, S.I., Zinovieva, R.D., Dolgilevich, S.M., Luchin, S.V., Krayev, A.S., Skryabin, K.G. Gause, G.G. (1984) FEBS Lett. 171, 297-302] show 77% without deletions/additions. result suggests lens synthase.