Heparin Derivatives of High Molecular Weight

Author(s):  
L. MESTER ◽  
A. AMIT AMAYA ◽  
M. MESTER
1977 ◽  
Author(s):  
R. von Hugo ◽  
R. Hafter ◽  
A. Stemberger ◽  
H. Graeff

Crosslinked high molecular weight derivatives of fibrin (fibrinoligomers) were observed during intravascular coagulation. It was the purpose of this study to investigate the complex formation of fibrin oligomers with fibrinogen and fibrinmonomer. Fibrinogen coupled to agarose (Fg-ag) as well as fi-brinmonomer coupled to agarose (Fm-ag) was used as substrate. Soluble oligomers of fibrin were produced by incubating fibrinogen with thrombin, calcium-chloride, cystein and F XIII. They were separated from fibrinogen by gel filtration. Γ-dimers were demonstrated in fractions from the void volume and the shoulder prior to the fibrinogen peak. These fractions were subjected to affinity chromatography. Crosslinked oligomers of fibrin were not adsorbed on Fg-ag, yet adsorption occured on Fm-ag. This indicates that fibrin oligomers have no affinity to fibrinogen, yet readily form complexes with fibrin. This could mean that in vivo they compete with fibrinogen for the fibrinmonomer part of soluble fibrin monomer complexes, and hence have a tendency to increase in size.


2021 ◽  
Vol 28 (10) ◽  
Author(s):  
A. H. Rojas-Calva ◽  
O. J. Hernández-Ortiz ◽  
F. M. Muñoz-Pérez ◽  
G. M. Estrada-Villegas ◽  
J. G. Ortega-Mendoza ◽  
...  

1978 ◽  
pp. 399-400 ◽  
Author(s):  
B. Dolabdjian ◽  
G. Grenner ◽  
P. Kirch ◽  
H.-L. Schmidt

1953 ◽  
Vol 51 (1) ◽  
pp. 140-144 ◽  
Author(s):  
J. Gordon

1. Glycine, alanine, and several isomers of alanine, DL-glutamic acid and DL-aspartic acid, when added to fresh guinea-pig serum and allowed to stand on the bench for half an hour, will protect the complement of this serum from destruction by heating at 55 and 56° C. for half an hour, but most of the complement activity is destroyed by heating at 57° C. and it is completely destroyed at 58° C. after half an hour.2. Derivatives of glycine do not have any protective effect.3. Various substances of high molecular weight, that might be described as ‘protective colloids’ do not have any protective effect.4. How these amino-acids when added to serum alter the heat-lability of the complement is not understood.


1955 ◽  
Vol 38 (4) ◽  
pp. 459-473 ◽  
Author(s):  
Barry Commoner ◽  
Mas Yamada

1. Exhaustive fractionation of leaves from tobacco plants systemically infected with TMV has led to the isolation of two non-virus proteins, B3 and B6, and the detection of a third, A4, which do not occur in comparable uninfected plants. 2. Components B3 and B6 have been found consistently in a series of ten extracts from plants grown over an 18 month period in all seasons of the year. It is concluded that these components are as characteristic of the infected plant as TMV itself. 3. As they occur in the initial extracts, the non-virus proteins are of low molecular weight (S20 ca. 3). On treatment, each component tends to form a high molecular weight polymer with an electrophoretic mobility considerably greater than that of the starting material. The high molecular weight derivatives of A4, B3, and B6 have been designated A8, B8, and B7 respectively. There is no evidence that these high molecular weight components occur as such in the infected leaf. 4. The non-virus proteins are free of nucleic acid and are not infectious. They cross-react immunochemically with TMV. 5. Compared with TMV content, the amounts of the non-virus proteins found in infected leaf are relatively small, falling in the range of 10 to 150 micrograms per gm. of tissue.


1994 ◽  
Vol 27 (7) ◽  
pp. 1981-1982 ◽  
Author(s):  
Duygu Avci ◽  
Selim H. Kusefoglu ◽  
Robert D. Thompson ◽  
Lon J. Mathias

1985 ◽  
Vol 53 (01) ◽  
pp. 080-085 ◽  
Author(s):  
A N Whitaker ◽  
J R McFarlane ◽  
E A Rowe ◽  
K Lee ◽  
P P Masci

SummaryWe have devised a simple enzyme immunoassay to detect and quantitate autoantibodies against derivatives of fibrinogen. This assay has been applied with a range of antigens including a fibrinogen lysate (containing X, Y, D and E), D dimer, D dimerE and a preparation of high molecular weight complexes derived from crosslinked fibrin. We have found that autoantibodies interacting with these antigens can be detected in varying concentrations in most sera from both normal subjects and patients with a variety of diseases and are evidently of mixed Ig class. These autoantibodies are directed against at least several cryptic antigens which appear during fibrinogen/fibrin degradation and some appear to be directed specifically against cross- linked fibrin derivatives. No clear disease correlates have yet emerged but a relationship between elevated levels and prior infective, thrombotic, inflammatory or traumatic disorders is likely. It is suggested that these autoantibodies may contribute to the catabolism of fibrinogen derivatives, provide a marker of thrombosis, and sometimes produce pathologic effects.


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