| | 1 | Author
| | Requires cookie* | | | Title
| Pierre Mermier  | | | | Abstract
| Association The competition dialysis is based on the competition for a ligand between a macromolecule and an excess of another molecule able to form a diffusible complex with this ligand. The procedure used the Colowick's cell and is proposed for determining association constants of complexes which contain tightly bound or labile apoproteins. | | | |
Reference
| (Z. Naturforsch. 30c, 534 [1975]; received May 14 1975) | | | |
Published
| 1975 | | | |
Keywords
| Constant, Complex, Metalloprotein, Flow Dialysis | | | |
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| default:Reihe_C/30/ZNC-1975-30c-0534_n.pdf | | | | Identifier
| ZNC-1975-30c-0534_n | | | | Volume
| 30 | |
| 3 | Author
| Ingrid Pilz, K. Arin Goral, FriedrichV D Haar | Requires cookie* | | | Title
| Phenylalanyl-tRNA Synthetase from Baker'Yeast: Structural Organization of the Enzyme and Its Complex with tRNAPhe as Determined by X-Ray Small-Angle Scattering | | | | Abstract
| The quaternary structure of the phenylalanyl-tRNA synthetase and its complex with tRNAPhe was studied in dilute solutions by small angle X-ray scattering. For the free synthetase the radius of gyration was determ ined as 5.5 nm, the volume 523 nm 3, the maximum diam eter 17.5 nm and the m olecular weight as 260 000 using an isopotential specific volume of 0.735. The overall shape could be best approxim ated by a flat cylinder with dimensions 18.2 n m X l l .5 n m X 4 nm ; the loose structure was approxim ated by building up the cylinder by spheres (diam eter 4.2 n m). The corresponding param eters of the enzyme tRN A complex were the following: radius of gyration 5.9 nm, volume 543 nm 3, maximum diam eter 21 nm and m olecular weight 290 000. These param eters suggest an 1:1 complex, whereby it m ust be assumed that the tRN A m olecule is attached in the extension of the longer axis. From the difference in the distance distribution functions of the free enzyme and the complex it is evident that we have to assume a change of conform ation (contraction) of the enzyme upon the binding of the specific tRNA. | | | |
Reference
| Z. Naturforsch. 34c, 20 (1979); received November 20 1978 | | | |
Published
| 1979 | | | |
Keywords
| X-Ray, Small-Angle, Scattering, Enzyme, Complex | | | |
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| default:Reihe_C/34/ZNC-1979-34c-0020.pdf | | | | Identifier
| ZNC-1979-34c-0020 | | | | Volume
| 34 | |
| 4 | Author
| Z. Naturforsch | Requires cookie* | | | Title
| The Rieske Protein from Purple Sulfur Bacteria Is an Extrinsic Protein | | | | Abstract
| The mode of membrane attachment of the Rieske iron-sulfur protein from cytochrome be, complex of Rhodospirillum rubrum has been studied using biochemical approaches. In contrast to cytochrome c, the bacterial Rieske protein was extracted from chromato-phores using chaotropic agents (NaSCN, urea, guanidine), an alkaline pH and relatively low concentration of Triton X-100. The results presented here lead to the conclusion, that the Rieske protein from chromato-phores is extrinsic and that their association with the rest of the complex involves hydropho bic interactions. In tro d u ctio n | | | |
Reference
| Z. Naturforsch. 53c, 15—20 (1998); received September 30/0ctober 16 1997 | | | |
Published
| 1998 | | | |
Keywords
| Chrom atophor, Cytochrome be, Complex, Rieske Protein, Rhodospirillum rubrum | | | |
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| default:Reihe_C/53/ZNC-1998-53c-0015.pdf | | | | Identifier
| ZNC-1998-53c-0015 | | | | Volume
| 53 | |
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