Purification of vitellogenin mRNA and serum albumin mRNA from avian liver by preparative gel electrophoresis.
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Biomedical subjects
Publications and source records attributed to J Mulder.
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The messenger RNA of the hormone-induced protein vitellogenin was isolated from the liver of estrogen-treated roosters. Starting from total polysomal RNA, the vitellogenin messenger was purified 67-fold by oligo (dT)-cellulose chromatography and sizing on a sucrose gradient. The messenger was translated in vitro into a 170 000 dalton polypeptide chain, having the immunochemical characteristics of vitellogenin. From electrophoretic and immunochemical analysis of the in vitro product of translation at least 63% of the messenger activity of the RNA preparation could be attributed to vitellogenin mRNA. Gel electrophoresis of the most purified fraction revealed residual contamination with the larger ribosomal RNA species. The molecular weight of the messenger RNA molecule, obtained by contour length measurements in the electron microscope, lies between 2.5 - 10(6) and 2.8 - 10(6).
The carboxyl-terminal tripeptide of casopressin (Pro-Arg-Gly.NH2) and adrenocorticotrophic hormone (ACTH) were injected intravenously into six human subjects, and the effects of these peptides on plasma free fatty acids (FFA) and cAMP concentrations were compared with that of saline. Twenty mug of the tripetide and 100 mug of ACTH INCREASED THE PLASMA FFA CONCENTRATION TO THE SAME EXTENT, WHEREAS 200 MUG OF THE TRIPETIDE WAS WITHOUT THIS LIPOLYTIC EFFECT. ACTH and the smaller dose of the tripeptide elevated the plasma cAMP level only in the same two subjects.
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