Characterization of neurophysin-vasopressin prohormones in human posterior pituitary tissue

The Journal of Clinical Endocrinology and Metabolism
J G Verbalis, A G Robinson

Abstract

To better characterize putative neurophysin-vasopressin prohormones in human posterior pituitary tissue, we extracted human posterior pituitary glands in 0.1 M HCl and isolated the higher molecular weight neurophysin-immunoreactive proteins. Sephadex G-75 gel filtration in 0.1 M formic acid with 6 M urea showed four distinct peaks of neurophysin immunoreactivity. Analysis of isolated lyophilized fractions of these peaks by sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed neurophysin-immunoreactive proteins at molecular weights of 10,000 daltons (79-87% of the total neurophysins), 19,000-20,000 daltons (10-16%), 26,000-30,000 daltons (1-2%), and a broad range of 30,000- to 100,000-dalton immunoreactivity from the void volume (V0) peak (2-3%). The 19,000- to 20,000-dalton and 26,000- to 30,000-dalton proteins were stable after both heating and treatment with reducing agents, but could be converted by chymotrypsin proteolysis to 10,000-dalton neurophysins and 3,000- to 5,000-dalton AVP-immunoreactive proteins. In contrast, the neurophysin immunoreactivity in the V0 peak was broken down to lower molecular weight neurophysin- and AVP-immunoreactive proteins by heating alone. Extraction of human posterior pituitarie...Continue Reading

Citations

Dec 7, 2005·Breast Cancer Research and Treatment·Brendan P KeeganWilliam G North
Sep 1, 1985·Peptides·F F CiarochiE A Zimmerman
Dec 1, 1990·Proceedings of the National Academy of Sciences of the United States of America·L C RosenbaumG Nilaver
Jun 1, 1991·Journal of Neuroendocrinology·J G VerbalisY P Loh
May 31, 2008·Expert Review of Cardiovascular Therapy·Jennifer E Ho, John R Teerlink
Jul 22, 1993·Annals of the New York Academy of Sciences·E Mohr, D Richter

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