Evolution of Neurophysin Proteins: The Partial Sequence of Bovine Neurophysin-I
- *Department of Microbiology, The Mount Sinai School of Medicine of the City University of New York, New York, N.Y. 10029
- †Department of Physiology, The Mount Sinai School of Medicine of the City University of New York, New York, N.Y. 10029
- ‡The Department of Biochemistry, Cornell University Medical College, New York, N.Y. 10021
Abstract
The sequence of the first 50 amino-acid residues of bovine neurophysin-I was determined. A comparison of this sequence with that of the 97-residue bovine neurophysin-II and the 92-residue porcine neurophysin-I molecules reveals a high degree of homology among these proteins. It is suggested that the binding site of neurophysin proteins for neurohypophyseal hormones is located in the middle portion of these molecules, where their sequences are virtually identical. The sequence data, as well as the occurrence of at least two neurophysins in both the pig and the cow, suggest that each species inherited at least two structural genes controlling the synthesis of these proteins. The most striking finding in the study was the observation of internal sequence homologies within the neurophysins. This result implies that these molecules arose by way of a series of partial gene duplications of a primitive gene that coded for a smaller ancestral protein.
