By John N. Abelson, Melvin I. Simon, David Barnes, Jennie P. Mather, Gordon H. Sato
This quantity comprises sections facing particular development elements within which new, up-to-date, or substitute systems are provided for purification, bioassay, radiolabeling and radioreceptor assay, immunoassay, receptor id, and quantification and comprises common innovations for the learn of progress components. For these unexpected with a selected quarter similar to the oncogene-growth issue courting orientation chapters were incorporated
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Extra resources for Peptide Growth Factors Part C
M. HILL Introduction Insulin-like growth factors I and II (IGF-I, IGF-II), as well as their specific receptors, have been identified and characterized in many tissues, including brain, by methods using whole cells and membrane preparations. H o w e v e r , the functions of these peptides and their receptors in brain are not yet known. We have used autoradiographic techniques to determine the anatomical distribution of the receptors in rat and chicken brain and in whole chick embryo. 1-3 The techniques for locating the IGF-I receptors have been adapted from the methods developed by H e r k e n h a m and Pert for the localization of drug and neurotransmitter receptors in fresh tissue 4 and were used by us previously to study brain insulin.
The identified area on the plate is isolated using the wide end of a Pasteur pipette. 5 g gelatin per liter) containing chloroform for sterility. In subsequent steps, the IGF-I receptor cDNA-containing hgtl0 phage are purified by repeated dilution, plating, and hybridization as described above. 8 (Fig. 2), which contains sequences c o m p l e m e n t a r y to probe 1. 8 and the synthetic probe derived from peptide 4 (Fig. 5 kilobases (kb), respectively. Complete nucleotide sequence analysis of the cloned cDNA resulted in deduction of the complete primary sequence of the human IGF-I receptor precursor (Fig.
Holmgren, M. Murby, B. Nilsson, S. Josephson, and M. Uhl6n, J. Biotechnol. 14, 423 (1990). 10 IGF, NGF, AND PDGF ll] expression o f IGFs in bacteria, owing to proteolysis in the cytoplasm and in the periplasm. 8'z9 In this study, each synthetic IGF gene was cloned into the p E Z Z I 8 expression plasmid as in-frame fusions to the Z Z structural gene. Thereafter, the nucleotide sequences at the junction of the Z Z gene and each I G F gene were mutagenized in vitro to introduce codons for amino acid residues furnishing cleavage sites to release mature IGF-I, tIGF-I, and IGF-II, respectively, from the Z Z - I G F fusion protein.
Peptide Growth Factors Part C by John N. Abelson, Melvin I. Simon, David Barnes, Jennie P. Mather, Gordon H. Sato