scholarly journals OBSERVATIONS ON THE PRESENCE OF A TOXIC SUBSTANCE IN THE BLOOD AND URINE OF PATIENTS WITH SCARLET FEVER

1924 ◽  
Vol 40 (3) ◽  
pp. 381-395 ◽  
Author(s):  
James D. Trask ◽  
Francis G. Blake

A series of observations on the blood of patients acutely ill with scarlet fever has shown that a toxic substance can be demonstrated in the serum by means of intracutaneous injections of the serum in persons who have not had scarlet fever and whose serums fail to blanch the rash in scarlet fever. The reaction caused by this substance consists of a bright red local erythema, varying from 20 to 70 mm. in diameter, of 1 to 4 days duration. The severer reactions are moderately indurated and tender, and are followed bypigmentation and desquamation. Control injections in persons whose serums blanch the rash in scarlet fever cause no reaction. The toxic substance is not neutralized by mixture with a human serum which gives a negative blanching test but is readily neutralized by a human serum which gives a positive blanching test. It is not neutralized by normal horse serum, but is completely neutralized by Dochez's scarlatinal antistreptococcic serum. In a limited number of observations on the urine of patients with scarlet fever a similar toxic substance has been found in two out of five cases studied. Since the toxic substance described appears to resemble the toxic substance found in the filtrates of scarlatinal hemolytic streptococcus cultures by Dick and Dick and since it is neutralized not only by a blanching human serum but also by Dochez's scarlatinal antistreptococcic horse serum, the experiments reported support the conception that scarlet fever is a local infection of the throat by a particular type of Streptococcus hæmolyticus capable of producing a toxin which is absorbed and is the cause of the general manifestations of the disease.

1942 ◽  
Vol 76 (5) ◽  
pp. 451-476 ◽  
Author(s):  
J. P. Henry

1. Normal horse serum was irradiated for periods of 3 to 4 days, with visible light or with ultraviolet light of known intensity and wave length. The photosensitizer hematoporphyrin was employed in some instances. The serum was exposed to the air in thin layers, and thoroughly agitated throughout irradiation. 2. The irradiated sera were unchanged in color, and over 90 per cent of the original protein content remained precipitable by phosphotungstic acid. 3. Studies of the antigenicity of the sera were carried out on guinea pigs and rabbits. Fresh antigenicities of deviated specificity and of an activity of the order of 1/50th, 1/1,000th, and less than 1/20,000th that of normal horse serum were obtained. The residual content of material having the same antigenic specificity as normal horse serum was estimated as approximately equivalent in activity to dilutions of normal horse serum of 1 cc., 1/10 cc., and less than 1/100 cc. per litre respectively.


1999 ◽  
Vol 43 (3) ◽  
pp. 655-660 ◽  
Author(s):  
Charles D. Sohaskey ◽  
Alan G. Barbour

ABSTRACT The spirochete Borrelia burgdorferi was unexpectedly found to be as susceptible to diacetyl chloramphenicol, the product of the enzyme chloramphenicol acetyltransferase, as it was to chloramphenicol itself. The susceptibilities of Escherichia coli and Bacillus subtilis, as well as that ofB. burgdorferi, to diacetyl chloramphenicol were then assayed in different media. All three species were susceptible to diacetyl chloramphenicol when growth media were supplemented with rabbit serum or, to a lesser extent, human serum. Susceptibility ofE. coli and B. subtilis to diacetyl chloramphenicol was not observed in the absence of serum, when horse serum was used, or when the rabbit or human serum was heated first. In the presence of 10% rabbit serum, a strain of E. colibearing the chloramphenicol acetyltransferase (cat) gene had a fourfold-lower resistance to chloramphenicol than in the absence of serum. A plate bioassay for chloramphenicol activity showed the conversion by rabbit, mouse, and human sera but not bacterial cell extracts or heated serum of diacetyl chloramphenicol to an inhibitory compound. Deacetylation of acetyl chloramphenicol by serum components was demonstrated by using fluorescent substrates and thin-layer chromatography. These studies indicate that esterases of serum can convert diacetyl chloramphenicol back to an active antibiotic, and thus, in vitro findings may not accurately reflect the level of chloramphenicol resistance by cat-bearing bacteria in vivo.


2013 ◽  
Vol 26 (1) ◽  
pp. 62-63 ◽  
Author(s):  
Anna Prigitano ◽  
Maria Carmela Esposto ◽  
Anna Maria Tortorano
Keyword(s):  

1948 ◽  
Vol 87 (1) ◽  
pp. 57-70 ◽  
Author(s):  
T. N. Harris

Complement-fixing antibodies to the cytoplasmic particles (CP) and to the S fraction of streptococcal nucleoproteins are present in normal human sera, the range of concentrations varying among the age groups. The titer of these antibodies rises between the first half-week and the 3rd week of scarlet fever, in more than 80 per cent of the cases. The titers then remain elevated for at least 4 months. In children, 91 per cent of the normal sera examined showed anti-CP titers up to 32; 87 per cent of sera in active rheumatic disease had titers above this level. Corresponding data with S fell in the same range of percentage distribution. Anti-CP and anti-S titers remained elevated long after the rheumatic process had reached quiescence. No correlation of serologic titer with the degree of clinical activity was found in the case of either antibody.


1937 ◽  
Vol 66 (2) ◽  
pp. 191-205 ◽  
Author(s):  
Walther F. Goebel ◽  
Rollin D. Hotchkiss

1. Azoprotein antigens containing glucuronic and galacturonic acids give rise in rabbits to specific antibodies. The immune sera show no serological crossing with antigens containing glucose or galactose. 2. The galacturonic acid antigen reacts in antipneumococcus horse serum Type I in high dilutions. 3. Azoprotein antigens containing galacturonic acid, benzene sulfonic and carboxylic acids precipitate in antipneumococcus horse sera of various types but not in normal horse serum. The mechanism underlying these cross reactions is discussed.


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