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. 1972 Feb;69(2):431-4.
doi: 10.1073/pnas.69.2.431.

Evolution of neurophysin proteins: the partial sequence of bovine neurophysin-I (vasopressin-oxytocin-carrier proteins-automated amino-acid-sequence analysis-homology-protein evolution)

Evolution of neurophysin proteins: the partial sequence of bovine neurophysin-I (vasopressin-oxytocin-carrier proteins-automated amino-acid-sequence analysis-homology-protein evolution)

J D Capra et al. Proc Natl Acad Sci U S A. 1972 Feb.

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.

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