Atypical incorporation of single amino acids into myelin proteins
| Autor: | J. D. Johnson, Francis Binkley, Neva King |
|---|---|
| Rok vydání: | 1976 |
| Předmět: |
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Lysine Nerve Tissue Proteins Cycloheximide Biochemistry Cellular and Molecular Neuroscience chemistry.chemical_compound Myelin Adenosine Triphosphate Ribonucleases Leucine medicine Animals Ribonuclease Amino Acids Myelin Sheath chemistry.chemical_classification biology Brain Amino acid Anti-Bacterial Agents Rats Kinetics medicine.anatomical_structure chemistry Puromycin Rats Inbred Lew biology.protein |
| Zdroj: | Journal of neurochemistry. 26(2) |
| ISSN: | 0022-3042 |
| Popis: | —Purified myelin incorporated l-[14C]leucine and l-[14C]lysine into myelin proteins in an enzymatic process similar to that of renal brush border membranes. The system was not inhibited by cycloheximide or puromycin or by pretreatment with ribonuclease; the reaction was inhibited by cetophenicol. ATP was an effector, shifting the optimal pH from 7.2 to 8.3. In the presence of ATP, myelin was less dense in a sucrose gradient. Ammonia was released from the membrane during the incorporation of amino acids. Myelin preloaded with cold leucine did not incorporate [14C]leucine but did incorporate [14C]lysine; there was no cross inhibition between the two amino acids. The incorporation was into or onto proteins of the Wolfgram proteolipid fraction of myelin. The incorporation was of the high affinity type with a Km of 10−7m and was restricted to the natural amino acids. |
| Databáze: | OpenAIRE |
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