
doi: 10.1007/bf01919637
pmid: 4442509
Futterung vonl-Valyl-(1-14C)-l-valyl-l-prolin anClaviceps purpurea und Abbau des erhaltenen Ergocornins und Ergokryptins zeigt, dass dieses Tripeptid, ebenso wie andere fruher untersuchte Peptide, sehr wahrscheinlich kein freies Zwischenprodukt in der Biogenese der Mutterkornalkaloide vom Peptidtyp ist. Es wird vorgeschlagen, dass die Biosynthese dieser Peptidalkaloide bis zur Stufe eines (d-Lysergyl-l-valyl)-l-valyl(oder leucyl)-l-prolin-lactams an einem Multienzym-Komplex ohne freie Zwischenprodukte ablauft.
Ergot Alkaloids, Peptide Chain Elongation, Translational, Carbon Radioisotopes, Amino Acids, Claviceps
Ergot Alkaloids, Peptide Chain Elongation, Translational, Carbon Radioisotopes, Amino Acids, Claviceps
| selected citations These citations are derived from selected sources. This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 40 | |
| popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network. | Average | |
| influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Top 10% | |
| impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Top 10% |
