Abstract
Biochemical study of the neurophysins, hypothalamo-neurohypophyseal protein carriers of the neuropeptide hormones oxytocin and vasopressin (Breslow, 1979), has focused on fundamental questions about the biosyn-thetic and molecular events by which these species are formed and stabilized into noncovalent complexes (see Fig. 1). While interacting complexes can be formed between native protein and hormone in their isolated forms, it has become evident from several properties of these molecules that bio-synthetic assembly is more complex. For example, unlike most proteins that remain close to their intact biosynthesized states after translation, neurophysins do not themselves contain sufficient amino acid sequence information to code for spontaneous folding to functional forms. When these proteins, which are highly disulfide cross-linked (seven disulfides per protein molecule of 10,000 daltons), are treated with “catalytic” (substoichio-metric) amounts of disulfide-reducing agent, they are inactivated readily, due to scrambling of the disulfides to nonnative combinations (Chaiken et al., 1975). Further, this process is speeded up by the inclusion of microsomal disulfide interchange enzyme.
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© 1982 Plenum Press, New York
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Chaiken, I.M., Fischer, E.A., Giudice, L.C., Hough, C.J. (1982). In Vitro Synthesis of Hypothalamic Neurophysin Precursors. In: McKerns, K.W., Pantić, V. (eds) Hormonally Active Brain Peptides. Biochemical Endocrinology. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-9248-8_16
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DOI: https://doi.org/10.1007/978-1-4615-9248-8_16
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