Go toArchive
Browse byFacets
Bookbag ( 0 )
'Complex' in keywords Facet   section ZfN Section C  [X]
Results  4 Items
Sorted by   
Publication Year
1998 (1)
1979 (1)
1975 (2)
1Author    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 
  Similar Items    Find
 TEI-XML for    default:Reihe_C/30/ZNC-1975-30c-0534_n.pdf 
 Identifier    ZNC-1975-30c-0534_n 
 Volume    30 
2Author    P. ScoppaRequires cookie*
 Title    Cadmium-Isocitrate Complex: Its Stability as a Function of Ionic Strength  
 Abstract    The complexation of cadmium by isocitrate has been studied at 25 °C and pH 7.5 in a range of ionic strength from 0.01 to 0 j16. The formation constant of the complex between cadmium and tribasic isocitrate varies from 860 M -1 at ^ = 0 .1 6 to approximately 24,500 M -1 at infinite dilu­ tion. These data allow the distribution of the chemical forms of cadmium added to the incubation mixtures for the assay of NAD-dependent isocitrate dehydrogenase to be calculated. 
  Reference    (Z. Naturforsch. 30c, 555 [1975]; received May 2 1975) 
  Published    1975 
  Keywords    Isocitrate Dehydrogenase, Isocitrate, Cadmium, Complexes, Ionic Strength 
  Similar Items    Find
 TEI-XML for    default:Reihe_C/30/ZNC-1975-30c-0555.pdf 
 Identifier    ZNC-1975-30c-0555 
 Volume    30 
3Author    Ingrid Pilz, K. Arin Goral, FriedrichV D HaarRequires 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 
  Similar Items    Find
 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-0020.pdf 
 Identifier    ZNC-1979-34c-0020 
 Volume    34 
4Author    Z. NaturforschRequires 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 
  Similar Items    Find
 TEI-XML for    default:Reihe_C/53/ZNC-1998-53c-0015.pdf 
 Identifier    ZNC-1998-53c-0015 
 Volume    53