An Acrylamide Gel Recombination Assay for Glycoprotein Hormone Subunits
| Autor: | Sheldon Schlaff |
|---|---|
| Rok vydání: | 1976 |
| Předmět: |
chemistry.chemical_classification
Protein Conformation Sodium Protein subunit Sodium Dodecyl Sulfate Thyrotropin chemistry.chemical_element Biological activity Luteinizing Hormone Chorionic Gonadotropin Molecular biology Iodine Radioisotopes Endocrinology chemistry Biochemistry Electrophoresis Polyacrylamide Gel Follicle Stimulating Hormone Glycoprotein Polyacrylamide gel electrophoresis Sodium dodecylsulfate Recombination Hormone |
| Zdroj: | Endocrinology. 98:527-533 |
| ISSN: | 1945-7170 0013-7227 |
| DOI: | 10.1210/endo-98-2-527 |
| Popis: | A specific and sensitive assay for recombination of the subunits of hCG and other glycoprotein hormones (LH, FSH, and TSH) is presented. The assay depends on the ability of sodium dodecylsulfate polyacrylamide gel electrophoresis (SDS-PAGE) to separate clearly the subunits from native hormone. Iodinated subunit is incubated with its identical unlabeled subunit and complementary subunit. Quantitative displacement of the radioactivity to the native hormone position as followed by gel slicing is used as a direct index of recombination. The assay is reproducible, sensitive to less than one picomole of hormone formed, and offers a simple means of evaluating recombination of glycoprotein chains as distinct from biological activity. (Endocrinology 98: 527, 1976) |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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