In vitro synthesis of peroxisomal membrane polypeptides
Peroxisomal membranes containing predominantly integral peroxisome membrane polypeptides were obtained from a highly purified peroxisomal fraction. Following sodium dodecylsulfate polyacrylamide gel electrophoresis three polypeptides with apparent molecular weights of 69, 36, and 22 kDa were isolate...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1986-06, Vol.137 (2), p.626-632 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Köster, Andrea Heisig, Michael Heinrich, Peter C. Just, Wilhelm W. |
| description | Peroxisomal membranes containing predominantly integral peroxisome membrane polypeptides were obtained from a highly purified peroxisomal fraction. Following sodium dodecylsulfate polyacrylamide gel electrophoresis three polypeptides with apparent molecular weights of 69, 36, and 22 kDa were isolated and used to raise antibodies in rabbits. Cell - free synthesis of these polypeptides was carried out in an in vitro translational system derived from rabbit reticulocytes. By subjecting peroxisomal membranes to reductive methylation [14C]-radiolabeled mature membrane polypeptides were obtained. The comparison of the three mature integral peroxisome membrane polypeptides with their corresponding in vitro synthesis products revealed no size differences indicating the lack of recognizable presequences for these peroxisomal membrane polypeptides. |
| doi_str_mv | 10.1016/0006-291X(86)91124-1 |
| format | Article |
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Following sodium dodecylsulfate polyacrylamide gel electrophoresis three polypeptides with apparent molecular weights of 69, 36, and 22 kDa were isolated and used to raise antibodies in rabbits. Cell - free synthesis of these polypeptides was carried out in an in vitro translational system derived from rabbit reticulocytes. By subjecting peroxisomal membranes to reductive methylation [14C]-radiolabeled mature membrane polypeptides were obtained. 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Following sodium dodecylsulfate polyacrylamide gel electrophoresis three polypeptides with apparent molecular weights of 69, 36, and 22 kDa were isolated and used to raise antibodies in rabbits. Cell - free synthesis of these polypeptides was carried out in an in vitro translational system derived from rabbit reticulocytes. By subjecting peroxisomal membranes to reductive methylation [14C]-radiolabeled mature membrane polypeptides were obtained. The comparison of the three mature integral peroxisome membrane polypeptides with their corresponding in vitro synthesis products revealed no size differences indicating the lack of recognizable presequences for these peroxisomal membrane polypeptides.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>2425798</pmid><doi>10.1016/0006-291X(86)91124-1</doi><tpages>7</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1986-06, Vol.137 (2), p.626-632 |
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| language | eng |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Animals Applied sciences Electrophoresis, Polyacrylamide Gel Exact sciences and technology Immune Sera - immunology In Vitro Techniques Liver - metabolism Membrane Proteins - biosynthesis Membrane Proteins - immunology Microbodies - metabolism Molecular Weight Other techniques and industries Poly A - metabolism Protein Biosynthesis Rabbits Rats RNA - metabolism RNA, Messenger |
| title | In vitro synthesis of peroxisomal membrane polypeptides |
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