Electron microscopy of fibrin Paris I

Blood ◽  
1980 ◽  
Vol 56 (1) ◽  
pp. 80-83 ◽  
Author(s):  
MW Mosesson ◽  
G Feldmann ◽  
D Menache
Keyword(s):  
Electron Microscopy ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Structural Abnormality ◽  
Clot Retraction ◽  
Gamma Chain ◽  
Crosslinking Site ◽  
Sterically Hindered

Abstract Fibrinogen Paris I, a congenital fibrinogen abnormality, is characterized by delayed fibrin aggregation and poor clot retraction owing to the replacement of normal gamma-chains by mutant gamma-chains, which are termed gamma-Paris I. Available evidence indicates that the structural abnormality involves the amino acid sequence near the COOH- terminus of the mutant chain and probably includes the region containing the normal gamma-chain crosslinking site. Electron microscopy was carried out on Paris I fibrin. In place of the normally interwoven network of branching cross-striated fibers, negatively or positively contrasted Paris I fibrin was characterized by nonfibrous clumps of material connected by distince fibrous strands tending to be thinner and more irregular in width than normal fibrin. Most Paris I fibrin fibers tended to the aperiodic, although cross-striations were observed occasionally in negatively contrasted specimens and rarely in positively contrasted specimens. In addition, Paris I fibrin frequently showed relatively short, abruptly terminating fibers. The gross ultrastructural differences between normal and Paris I fibrin suggest that for fibrin assembly to take place normally, a region(s) in the fibrin molecule near to or possibly overlapping the COOH-terminal gamma- chain crosslinking site must be preserved or at least not sterically hindered.

Cellular imaging and mitochondria targeted photo-cytotoxicity in visible light by singlet oxygen using a BODIPY-appended oxovanadium(iv) DNA crosslinking agent

MedChemComm ◽  
2016 ◽  
Vol 7 (7) ◽  
pp. 1398-1404 ◽  
Author(s):  
Arun Kumar ◽  
Akanksha Dixit ◽  
Samya Banerjee ◽  
Arnab Bhattacharyya ◽  
Aditya Garai ◽  
...  
Keyword(s):  
Visible Light ◽  
Singlet Oxygen ◽  
Crosslinking Agent ◽  
Cellular Imaging ◽  
Dna Crosslinking ◽  
Crosslinking Site

Targeted PDT by1O2at mtDNA crosslinking site of a BODIPY-appended VO2+complex in visible light.

scholarly journals Electron microscopy of fibrin Paris I

Blood ◽  
1980 ◽  
Vol 56 (1) ◽  
pp. 80-83
Author(s):  
MW Mosesson ◽  
G Feldmann ◽  
D Menache
Keyword(s):  
Electron Microscopy ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Structural Abnormality ◽  
Clot Retraction ◽  
Gamma Chain ◽  
Crosslinking Site ◽  
Sterically Hindered

Fibrinogen Paris I, a congenital fibrinogen abnormality, is characterized by delayed fibrin aggregation and poor clot retraction owing to the replacement of normal gamma-chains by mutant gamma-chains, which are termed gamma-Paris I. Available evidence indicates that the structural abnormality involves the amino acid sequence near the COOH- terminus of the mutant chain and probably includes the region containing the normal gamma-chain crosslinking site. Electron microscopy was carried out on Paris I fibrin. In place of the normally interwoven network of branching cross-striated fibers, negatively or positively contrasted Paris I fibrin was characterized by nonfibrous clumps of material connected by distince fibrous strands tending to be thinner and more irregular in width than normal fibrin. Most Paris I fibrin fibers tended to the aperiodic, although cross-striations were observed occasionally in negatively contrasted specimens and rarely in positively contrasted specimens. In addition, Paris I fibrin frequently showed relatively short, abruptly terminating fibers. The gross ultrastructural differences between normal and Paris I fibrin suggest that for fibrin assembly to take place normally, a region(s) in the fibrin molecule near to or possibly overlapping the COOH-terminal gamma- chain crosslinking site must be preserved or at least not sterically hindered.

Crosslinking Site

2016 ◽  
Author(s):  
J. Alemán ◽  
A. V. Chadwick ◽  
J. He ◽  
M. Hess ◽  
K. Horie ◽  
...  
Keyword(s):  
Crosslinking Site

Sequence location of a putative transglutaminase crosslinking site in human α2 -macroglobulin

FEBS Letters ◽  
1981 ◽  
Vol 129 (2) ◽  
pp. 314-317 ◽  
Author(s):  
Steen B. Mortensen ◽  
Lars Sottrup-Jensen ◽  
H. Frede Hansen ◽  
Diane Rider ◽  
Torben E. Petersen ◽  
...  
Keyword(s):  
Α2 Macroglobulin ◽  
Crosslinking Site

Optimizing the Photocontrol of bZIP Coiled Coils with Azobenzene Crosslinkers: Role of the Crosslinking Site

ChemBioChem ◽  
2015 ◽  
Vol 16 (12) ◽  
pp. 1757-1763 ◽  
Author(s):  
Ahmed M. Ali ◽  
Matthew W. Forbes ◽  
G. Andrew Woolley
Keyword(s):  
Coiled Coils ◽  
Crosslinking Site

Alkaline hydrolysis of pivalic esters of ethylene glycol in water-acetone solutions

1980 ◽  
Vol 45 (3) ◽  
pp. 720-726 ◽  
Author(s):  
Stanislav Ševčík ◽  
Miroslav Kubín ◽  
Jiří Štamberg
Keyword(s):  
Ethylene Glycol ◽  
Alkaline Hydrolysis ◽  
Structural Unit ◽  
Hydroxyethyl Methacrylate ◽  
Structural Units ◽  
Kinetics Of Hydrolysis ◽  
Ethylene Dimethacrylate ◽  
Crosslinking Site ◽  
Kinetics Of ◽  
Hydrolysis Of

The paper reports alkaline hydrolysis of ethylene dipivalate and 2-hydroxyethyl pivalates as compounds modelling the structural unit and crosslinking site of hydrophilic gels, i.e. copolymers of 2-hydroxyethyl methacrylate and ethylene dimethacrylate. The kinetics of hydrolysis was investigated in water-acetone solutions containing respectively 50, 75, 80, 85 and 90% by vol. (related to 20°C) of acetone at 20, 30, 40, and 50°C. It was demonstrated that, owing to steric hindrance, the preferential hydrolysis of monoester was more pronounced in the case of pivalic esters of ethylene glycol compared with acetic esters of ethylene glycol. The results are discussed in connection with the selectivity of the alkaline hydrolysis of ester bonds in "pendant" parts of structural units in hydrophylic methacrylate gels.

CONFORMATIONAL EQUILIBRIA IN THE γ CHAIN COOH-TERMINUS OF HUMAN FIBRINOGEN

1987 ◽  
Author(s):  
C S Cierniewski ◽  
A Z Budzynski
Keyword(s):  
Binding Sites ◽  
Synthetic Peptide ◽  
Native Structure ◽  
Native Conformation ◽  
Human Fibrinogen ◽  
Long Range Interactions ◽  
Conformational Equilibria ◽  
Crosslinking Site ◽  
Antibody Population

Synthetic peptides and fragments cleaved from native fibrinogen are used in studies to localize binding sites for various ligands. We addressed the question how the native conformation of a selected γ chain segment is affected by scission of the original chain. The conformation of the γ chain COOH-terminus of intact fibrinogen and its various fragments containing this region has been compared by an immunochemical analysis. An antibody population specific for the native epitope within the γ391-405 segment was isolated by affinity chromatography on the corresponding synthetic peptide. Between 19.2 and 22.8% of antibodies were obtained from three different antisera indicating that this region represents one of the major epitopes of native fibrinogen. Anti-γ391-405 antibodies were used to determine the value of Kconf the equilibrium constant for the interconversion of the non-native and native conformations of this epitope. The measurements were done using native fibrinogen, fragments D1 and DD, γ chain and γ391-405 synthetic peptide. In addition, the effect of 5 M guanidine-HCl on the conformation of fragments D1 and DD, which is known to abolish their antipolymerizing activity, was studied. Radioiodinated fibrinogen was used in the determination of Kconf, and quantitative analytical parameters, CI50% and CIs, calculated from competition between 125I-fibrinogen and the fibrinogen derivatives under study for binding to the immunochemically purified antibody. The measurements indicated that the epitope is unperturbed by iodination of fibrinogen and that 38.3% of fragment D1, 8.9% of fragment DD, 3.6% of the γ chain and less than 0.008% of the γ391-405 molecules adopt in aqueous solution the native conformation within the epitope. Denaturation of fragment D1 with 5 M guanidine-HCl affected only slightly the conformation of this γ chain determinant. More significant changes in the conformation were observed when fragment DD was denatured. The results suggest that long-range interactions are necessary for the stabilization of the native structure in the region of fibrinogen that interacts with the antibody and which is in close vicinity to the polymerization site, crosslinking site, and platelet recognition site.

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