scholarly journals THE NATURE OF THE VIRUS RECEPTORS OF RED CELLS

1949 ◽  
Vol 89 (2) ◽  
pp. 223-232 ◽  
Author(s):  
George K. Hirst

A substance (VHI) exists in human plasma which inhibits the agglutination of red cells by influenza virus and is distinct from influenza antibody. When plasma is fractionated by alcohol in the cold the VHI comes out mainly with a mixture of lipid-free alpha and beta globulins (fraction IV-4). On further fractionation the activity comes out with a fraction consisting mainly of beta1 globulin (fraction IV-7). Boiling fraction IV-4 or IV-7 after considerable dilution brings about a large increase in the amount of VHI, much more than can be detected in the original plasma. A similar VHI has been extracted from the ghosts of fowl red cells.

1948 ◽  
Vol 87 (4) ◽  
pp. 315-328 ◽  
Author(s):  
George K. Hirst

Evidence has been offered that influenza virus which has been heated at 56°C. for 30 or more minutes loses some of its capacity to agglutinate red cells and may completely lose its power to elute from cells on which it has been adsorbed. Such heat-inactivated virus does not possess the capacity to destroy the virus inhibitor in normal rabbit serum and this appears to be the explanation of the higher agglutinin inhibitory levels obtained with serum and heated virus as compared with serum and untreated virus. The heat-inactivated virus can be used to measure the inhibitor substance in normal rabbit serum. By two different methods it has been demonstrated that the inhibitor is destroyed in the presence of unheated influenza virus, as measured by inhibition titrations with virus inactivated at 56°C. The destruction of inhibitor by virus of either type A or B can be measured by virus of either type with similar results.


1949 ◽  
Vol 89 (2) ◽  
pp. 233-243 ◽  
Author(s):  
George K. Hirst

Influenza virus, treated with sodium periodate, was adsorbed well on red cells but lacked the capacity for spontaneous elution. Heated virus was eluted from red cells by the action of cholera vibrio filtrate, unheated influenza virus, and to a small extent by heating at 56°C. Periodate-treated virus was not elutable by these methods but was liberated by exposure of the adsorbing cells to concentrations of sodium chloride of 5 to 10 per cent. This treatment had no effect on elution of heated virus.


1948 ◽  
Vol 87 (4) ◽  
pp. 301-314 ◽  
Author(s):  
George K. Hirst

The influenza virus receptors of fowl red cells and the influenza virus inhibitor of normal rabbit serum have the following attributes in common: They are stable at high temperatures and in solutions of pH as high as 10.0. They both resist destruction by a number of oxidizing agents but are readily destroyed by sodium periodate, trypsin, and influenza virus. These facts suggest that the red cell receptor and the normal serum inhibitor are either the same or analogous substances and that they may belong to the mucoprotein class of compounds.


1950 ◽  
Vol 91 (2) ◽  
pp. 161-175 ◽  
Author(s):  
George K. Hirst

A strain each of mumps and Newcastle disease virus and five strains of influenza virus were found to be capable of removing all the receptors for this group of viruses from fowl red cells. Five virus strains were tested for their capacity to inactivate the virus hemagglutinin of human plasma and of egg white. In the case of egg white all strains including mumps and Newcastle disease virus inactivated the inhibitor completely, or nearly so. With plasma the influenza strains inactivated the inhibitor completely but mumps and NDV destroyed only that portion of the complex which effected mumps inhibition. The inhibitor for some strains was destroyed more rapidly than that for others and the sequence in which they were destroyed (inhibitor gradient) was similar, regardless of the strain employed. The inhibitor gradient for egg white was very different from that for plasma and these in turn differed significantly from the receptor gradient for fowl red cells.


2009 ◽  
Vol 33 (8) ◽  
pp. 895-903 ◽  
Author(s):  
Zhang-Yong Ning ◽  
Min-Yi Luo ◽  
Wen-Bao Qi ◽  
Bo Yu ◽  
Pei-Rong Jiao ◽  
...  

1950 ◽  
Vol 91 (2) ◽  
pp. 123-133 ◽  
Author(s):  
Oscar D. Ratnoff ◽  
Robert C. Hartmann ◽  
C. Lockard Conley

A fraction of globulin was prepared from human plasma which was deficient in prothrombin, thrombin, fibrinogen, plasma thromboplastin, and accelerator globulin. The preparation of globulin contained considerable potential proteolytic activity which could be activated by streptococcal fibrinolysin. This fraction of globulin accelerated the clotting of normal platelet-deficient plasma. However, the clot-accelerating effect of the globulin fraction was the same whether or not its proteolytic property had been activated. The addition of streptococcal fibrinolysin to normal platelet-deficient plasma did not accelerate coagulation. Nor did the addition of streptococcal fibrinolysin to hemophilic platelet-deficient plasma promote its coagulation. The data presented suggest that proteolysis by activated plasma proteolytic enzyme is not an essential stage in the coagulation of the blood.


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