Refine
Has Fulltext
- yes (69) (remove)
Is part of the Bibliography
- yes (69)
Year of publication
- 1984 (69) (remove)
Document Type
- Journal article (50)
- Conference Proceeding (8)
- Book article / Book chapter (6)
- Book (2)
- Review (2)
- Jahresbericht (1)
Keywords
- Chemie (6)
- Toxikologie (6)
- Biochemie (4)
- Physiologische Chemie (4)
- Aufsatzsammlung (3)
- Anatolische Sprachen (2)
- Anorganische Chemie (2)
- Minoische Kultur (2)
- Mykenische Kultur (2)
- Neurospora crassa (2)
Institute
- Theodor-Boveri-Institut für Biowissenschaften (20)
- Institut für Anorganische Chemie (8)
- Institut für Pharmakologie und Toxikologie (8)
- Institut für Psychologie (bis Sept. 2007) (5)
- Neuphilologisches Institut - Moderne Fremdsprachen (bis 2007) (5)
- Institut für Organische Chemie (3)
- Institut für Psychologie (3)
- Institut für Slavistik (3)
- Institut für Altertumswissenschaften (2)
- Institut für Altertumswissenschaften (bis Sept. 2007) (2)
The purification and the amino acid sequence of a proteolipid translated on ribosomes in yeast mitochondria is reported. This protein, which is a subunit of the A TP synthase, was purified by extraction with chloroform/methanol (2/1) and subsequent chromatography on phosphocellulose and reverse phase h.p.l.c. A mol. wt. of 5500 was estimated by chromatography on Bio-Gel P-30 in 8011/o fonnie acid. The complete amino acid sequence of this protein was determined by automated solid phase Edman degradation of the whole protein and of fragments obtained after cleavage with cyanogen bromide. The sequence analysis indicates a length of 48 amino acid residues. The calculated mol. wt. of 5870 corresponds to the value found by gel chromatography. This polypeptide contains three basic residues and no negatively charged side chain. The three basic residues are clustered at the C terminus. The primary structure of this protein is in full agreement with the predicted amino acid sequence of the putative polypeptide encoded by the mitochondrial aap1 gene recently discovered in Saccharomyces cerevisiae. Moreover, this protein shows 5011/o homology with the amino acid sequence of a putative polypeptide encoded by an unidentified reading frame also discovered near the mitochondrial ATPase subunit 6 genein Aspergillus nidulans.
No abstract available
No abstract available
In den starren Molekülen 1- 10 reagieren die benachbarten parallelen C = C- und N = N-Bindungen nahezu quantitativ unter Photocyclisierung lU den l,2-Diazetidinen 11-10, deren Struktur spektroskopisch und für 13 durch Kristallstrukturanalyse bewiesen wird. Die in Abwesenheit der C = C-Bindung beobachtete Photo-Denitrogenierung unterbleibt selbst bei den empfindlichen Derivaten des 2,3-Diazabicyclo[2.2.11heptens. Photocyclisierung von 6 mit lwei zur N=N· Bindung benachbarten C=C-Bindungen tritt nur mit der Norbornendoppelbindung ein.
In addition to the endocrine effects, the thyrotropin releasing hormone (TRH) is known to induce dose-dependent increases in blood pressure and heart rate after intracerebroventricular (i.c.v.) administration in urethane-anaesthetised rats (1, 2). The a~ of the present study was to investigate whether TRH has similar effects in conscious rats of various strains i.e. spontaneously hypertensive rats (SHR), normotensive Wistar-Kyoto (WKY) and Wistar (NR) rats.
The binding of \([^3H]\)phenobarbital to rat brain membranes was studied in order to determine its characteristics and specificity. The binding reaction was rapid and occurred at sites of low affinity. \((K_d = 700 μM)\) and very high density \((B_{max} = 2.7 nmoll/mg protein)\). It was unaffected by temperature changes from O°C to 95°C and was maximal at pH 5. Detergents in low concentrations markedly decreased the binding, apparently without solubilizing the binding sites. It is concluded that the binding of \([^3H]\) phenobarbital is a rather non-specific interaction with the plasma membrane.
No abstract available.