Structural characterization of factor I mediated cleavage of the third component of complement

Biochemistry ◽  
1982 ◽  
Vol 21 (23) ◽  
pp. 5745-5749 ◽  
Author(s):  
Alvin E. Davis ◽  
Richard A. Harrison
Keyword(s):  
Structural Characterization ◽  
Factor I ◽  
The Third ◽  
Third Component Of Complement

scholarly journals Structural characterization of the third scavenger receptor cysteine‐rich domain of murine neurotrypsin

2019 ◽  
Vol 28 (4) ◽  
pp. 746-755 ◽  
Author(s):  
Anselmo Canciani ◽  
Gianluca Catucci ◽  
Federico Forneris
Keyword(s):  
Structural Characterization ◽  
Scavenger Receptor ◽  
The Third ◽  
Rich Domain ◽  
Cysteine Rich Domain

Detection and Structural Characterization of Natural Ara h 7, the Third Peanut Allergen of the 2S Albumin Family

2010 ◽  
Vol 9 (7) ◽  
pp. 3701-3709 ◽  
Author(s):  
Hendrik Schmidt ◽  
Susanne Krause ◽  
Christoph Gelhaus ◽  
Arnd Petersen ◽  
Ottmar Janssen ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Peanut Allergen ◽  
2S Albumin ◽  
The Third

scholarly journals A molybdenum tris(dithiolene) complex coordinates to three bound cobalt centers in three different ways

2019 ◽  
Vol 75 (8) ◽  
pp. 1261-1264
Author(s):  
Neilson Nguyen ◽  
Alan J. Lough ◽  
Ulrich Fekl
Keyword(s):  
Structural Characterization ◽  
Cobalt Atom ◽  
Main Group ◽  
Molecular Compound ◽  
Multidentate Ligand ◽  
The Third

The synthesis and structural characterization of the molecular compound (μ3-benzene-1,2-dithiolato)hexacarbonylbis(μ3-1,1,1,4,4,4-hexafluorobut-2-ene-2,3-dithiolato)tricobaltmolybdenum, [Co3Mo(C4F6S2)2(C6H4S2)(CO)6] or Mo(tfd)2(bdt)(Co(CO)2)3 (tfd is 1,1,1,4,4,4-hexafluorobut-2-ene-2,3-dithiolate and bdt is benzene-1,2-dithiolate), are reported. The structure of the molecule contains the molybdenum tris(dithiolene) complex Mo(tfd)2(bdt) coordinated as a multidentate ligand to three cobalt dicarbonyl units. Each of the three cobalt centers is relatively close to molybdenum, with Co...Mo distances of 2.7224 (7), 2.8058 (7), and 2.6320 (6) Å. Additionally, each of the cobalt centers is bound via main-group donor atoms, but each one in a different way: the first cobalt atom is coordinated by two sulfur atoms from different dithiolenes (bdt and tfd). The second cobalt atom is coordinated by one sulfur from one tfd and two olefinic carbons from another tfd. The third cobalt is coordinated by one sulfur from bdt and two sulfurs from tfd. This is, to the best of our knowledge, the first structurally characterized example of a molybdenum (tris)dithiolene complex that coordinates to cobalt. The F atoms of two of the –CF3 groups were refined as disordered over two sets of sites with ratios of refined occupancies of 0.703 (7):0.297 (7) and 0.72 (2):0.28 (2).

scholarly journals Theoretical study on the third-order nonlinear optical properties and structural characterization of 3-Acetyl-6-Bromocoumarin

2016 ◽  
Vol 653 ◽  
pp. 122-130 ◽  
Author(s):  
Adailton N. Castro ◽  
Leonardo R. Almeida ◽  
Murilo M. Anjos ◽  
Guilherme R. Oliveira ◽  
Hamilton B. Napolitano ◽  
...  
Keyword(s):  
Optical Properties ◽  
Structural Characterization ◽  
Nonlinear Optical ◽  
Theoretical Study ◽  
Nonlinear Optical Properties ◽  
Third Order ◽  
The Third

scholarly journals Analysis of the interactions between properdin, the third component of complement (C3), and its physiological activation products

1988 ◽  
Vol 252 (1) ◽  
pp. 47-54 ◽  
Author(s):  
T C Farries ◽  
P J Lachmann ◽  
R A Harrison
Keyword(s):  
Ionic Strength ◽  
Alternative Pathway ◽  
Fluid Phase ◽  
Complement C3 ◽  
Initial Product ◽  
Native Form ◽  
Factor I ◽  
The Third ◽  
Activation Products ◽  
Third Component Of Complement

The interactions of properdin with both surface-bound and fluid-phase C3 (the third component of complement) and its activation products have been investigated by using a purified preparation of the ‘native’ form. At physiological ionic strength, a weak interaction with cell-bound C3b (the larger activation fragment of C3) could be demonstrated. In the presence of Factor B this interaction was enhanced, and further enhancement was seen when C3bBb sites were formed on the erythrocytes. The avidities of properdin for cell-bound iC3b (the initial product of Factors I and H action on C3b) and C3b were compared at low ionic strength, with that measured for iC3b being less than that for C3b. In contrast, the affinities of properdin for fluid-phase C3b, iC3b and C3c (the larger product of Factors I and H or CR1 (the C3b receptor) action on iC3b) were all very similar, and apparently much weaker than that for cell-bound C3b. No interaction with either native C3 or, more surprisingly, C3i (haemolytically inactive C3) could be detected. Properdin also inhibited Factor I binding to, and action upon, cell-bound C3b, but did not inhibit Factor I action on fluid-phase C3b. These data permit a more detailed description of the roles of properdin in the alternative pathway of complement activation, emphasizing its importance in concentrating activation at the activating surface.

New ultrastructural findings about Borrelia burgdorferi by cryofixation, negative staining, thin sectioning and scanning techniques

1990 ◽  
Vol 48 (3) ◽  
pp. 582-583
Author(s):  
S. F. Hayes ◽  
M. D. Corwin ◽  
T. G. Schwan ◽  
D. W. Dorward ◽  
W. Burgdorfer
Keyword(s):  
Lyme Disease ◽  
Borrelia Burgdorferi ◽  
Structural Characterization ◽  
Negative Staining ◽  
Low Speed ◽  
Thin Sectioning ◽  
Ultrastructural Findings

Characterization of Borrelia burgdorferi strains by means of negative staining EM has become an integral part of many studies related to the biology of the Lyme disease organism. However, relying solely upon negative staining to compare new isolates with prototype B31 or other borreliae is often unsatisfactory. To obtain more satisfactory results, we have relied upon a correlative approach encompassing a variety EM techniques, i.e., scanning for topographical features and cryotomy, negative staining and thin sectioning to provide a more complete structural characterization of B. burgdorferi.For characterization, isolates of B. burgdorferi were cultured in BSK II media from which they were removed by low speed centrifugation. The sedimented borrelia were carefully resuspended in stabilizing buffer so as to preserve their features for scanning and negative staining. Alternatively, others were prepared for conventional thin sectioning and for cryotomy using modified procedures. For thin sectioning, the fixative described by Ito, et al.

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