The effect of therapeutic injections of horse serum on the bactericidal and anticomplementary activity of human serum

1939 ◽  
Vol 48 (1) ◽  
pp. 227-230 ◽  
Author(s):  
Scott Thomson
Keyword(s):  
Human Serum ◽  
Horse Serum ◽  
Anticomplementary Activity

scholarly journals Esterases in Serum-Containing Growth Media Counteract Chloramphenicol Acetyltransferase Activity In Vitro

1999 ◽  
Vol 43 (3) ◽  
pp. 655-660 ◽  
Author(s):  
Charles D. Sohaskey ◽  
Alan G. Barbour
Keyword(s):  
Human Serum ◽  
Horse Serum ◽  
Chloramphenicol Acetyltransferase ◽  
Rabbit Serum ◽  
Growth Media ◽  
Chloramphenicol Resistance ◽  
E Coli ◽  
Cell Extracts

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.

Comparison of effects of human serum and horse serum onin vitrosusceptibility testing of echinocandins

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

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
Keyword(s):  
Human Serum ◽  
Scarlet Fever ◽  
Horse Serum ◽  
Toxic Substance ◽  
Local Infection ◽  
Hemolytic Streptococcus ◽  
Normal Horse Serum

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.

The penetration of human epidermal sheets by the cercariae of Schistosoma mansoni and the collection of schistosomula

Parasitology ◽  
1970 ◽  
Vol 60 (1) ◽  
pp. 89-96 ◽  
Author(s):  
J. R. Kusel
Keyword(s):  
Sodium Chloride ◽  
Human Serum ◽  
Medical Research Council ◽  
Horse Serum ◽  
Red Cells ◽  
Yeast Cells ◽  
Human Epidermis ◽  
The University ◽  
Department Faculty ◽  
Percentage Conversion

1. The percentage conversion of cercariae into schistosomula, when the former were penetrating human epidermal sheets, was found not to be significantly affected by the underlying media 1—5 (Table 1). The percentage conversion varied from 16·4% (in normal saline underlying skin) to 26.2 %. When distilled water was the underlying medium significantly fewer cercariae penetrated the sheets.2. There was a statistically significant decrease in the percentage conversion of cercariae to schistosomula when sodium chloride final concentration 0·67 % was placed in the exposure tube with the cercariae (1·6 % P = < 0·02 when compared with La Ye medium); 0·43 % sodium chloride also significantly decreased penetration.3. There was a statistically significant decrease in the percentage conversion of cercariae to schistosomula when the orientation of the human epidermis was reversed, i.e. the biologically inner surface was exposed to the cercariae (2.6 %, P = < 0.02, when compared with La Ye medium).4. Schistosomula agglutinated in the presence of normal or immune human serum or horse serum. In human serum to which donor red blood cells had been added, many red cells adhered to the schistosomula. The number adhering was less in inactivated serum. The adhesion was specific for red cells, the effect not occurring with either yeast cells or silicic acid particles. The red cells were shed from the surface of the schistosomulum after 4—12 h.I should like to thank the following: Dr S. A. Ibrahim, in whose laboratory this work was carried out; Dr S. Dawood of the Stack Laboratory, Khartoum for the use of his microscope; Mr T. R. Melrose and Mr J. R. Lauder for valuable discussions; the Medical Research Council, U.K., and the University of Khartoum for research grants. I am very grateful to the Pathology Department Faculty of Medicine, University of Khartoum, for preparing the sections of human epidermis.

scholarly journals A Simple Method for the Preservation of Sera by Desiccation in the Frozen State Without the use of Refrigerants

1936 ◽  
Vol 36 (4) ◽  
pp. 507-513 ◽  
Author(s):  
R. I. N. Greaves ◽  
Muriel E. Adair
Keyword(s):  
Guinea Pig ◽  
Human Serum ◽  
Horse Serum ◽  
High Vacuum ◽  
Human Albumin ◽  
Vacuum Pump ◽  
Simple Method ◽  
Simple Process ◽  
Special Apparatus ◽  
Frozen State

SummaryA simple process is described for the desiccation of antisera after freezing by rapid evaporation. Freezing has been brought about by the rapid evaporation which takes place in a high vacuum in the presence of P2O5. The violent frothing which takes place when serum is exposed to a high vacuum has been controlled by a preliminary evacuation of the serum in the absence of the drying agent.No special apparatus except an efficient high vacuum pump is necessary for this process.This process has been applied for the preservation of (a) anti-horse serum, anti-ox serum, anti-human serum, anti-human globulin and anti-crystalline human albumin sera; (b) anti-sheep cell haemolysin; (c) guinea-pig complement; (d) various Salmonella antisera.Preliminary experiments are described of the application of this method to the drying of bacteria.We desire to thank Dr P. Hartley for his valuable advice and for showing us his paper prior to publication.

Influence of matrix on concentrations of somatotropin measured in serum with commercial immunoradiometric assays.

1989 ◽  
Vol 35 (7) ◽  
pp. 1423-1426 ◽  
Author(s):  
R A Felder ◽  
R W Holl ◽  
P Martha ◽  
G Bauler ◽  
P Hellman ◽  
...  
Keyword(s):  
Quality Control ◽  
Human Serum ◽  
Horse Serum ◽  
Human Growth ◽  
Reference Intervals ◽  
Genetically Engineered ◽  
Quality Control Material ◽  
Serum Samples ◽  
Control Material ◽  
Human Pituitary

Abstract Using immunoradiometric assays (IRMAs) from Hybritech Inc. (H) and Nichols Institute Diagnostics (ND), we measured somatotropin (human growth hormone, hGH) in serum samples obtained every 20 min for 24 h from 10 prepubertal subjects with short stature. Results obtained with the ND reagents were 2.74 times greater than those obtained with the H reagents (P = 0.00001, r = 0.94, SEE = 3.9, n = 720). We therefore compared the IRMAs with the standard hGH RIA from the National Institutes of Health (NIH) National Hormone and Pituitary Program, using the genetically engineered hGH preparations (from Genentech Inc.) 22-kDa hGH and methionated 20-kDa hGH. We also assayed human pituitary hGH (NIH, lot no. AFP-4793B). Each hGH preparation was diluted in three diluent buffer systems: horse serum from H and from ND, and human serum. The RIA and H-IRMA gave superimposable standard curves for all hGH preparations in each diluent. The methionated 20-kDa hGH was not detected in the H-assay. Use of human serum matrix in the ND-IRMA shifted the standard curve as compared with the horse-serum matrix, giving equivalent binding at lower concentrations; i.e., serum hGH was overestimated in samples assayed against standards diluted in horse serum. Quality-control materials (Ciba-Corning) yielded disparate results in all three assays, yet human serum pools containing hGH gave similar results in the H and the NIH assays, and higher values in ND. When a human serum standard was used in the ND assay, both IRMAs gave similar results to the RIA assay for human serum samples. Reference intervals for hGH should be determined by each analytical laboratory, to prevent misdiagnosis of patients. Furthermore, quality-control material should be of human origin, because commercially supplied quality-control material does not react the same as human serum in some hGH assays.

scholarly journals Use of procainamide gels in the purification of human and horse serum cholinesterases

1983 ◽  
Vol 211 (1) ◽  
pp. 243-250 ◽  
Author(s):  
J S Ralston ◽  
A R Main ◽  
B F Kilpatrick ◽  
A L Chasson
Keyword(s):  
Human Serum ◽  
Large Scale ◽  
Small Volume ◽  
Horse Serum ◽  
Retention Capacity ◽  
Relative Binding ◽  
Human Enzyme ◽  
Sepharose 4B ◽  
Human Cholinesterase

Two large-scale methods based primarily on the use of procainamide-Sepharose gels were developed for the purification of horse and human serum non-specific cholinesterases. With method I, the procainamide-Sepharose 4B gel was used in the first step to handle large volumes of serum. With method II, the procainamide-Sepharose 4B gel was used in the final step to obtain pure enzyme. Although both methods gave electrophoretically pure cholinesterase preparations in good yields, they were significantly more efficient at purifying the horse enzyme than the human enzyme. To study this problem, the relative binding of human and horse cholinesterases to procainamide-, methylacridinium (MAC)-, m-trimethylammoniophenyl (m-PTA)- and p-trimethylammoniophenyl (p-PTA)-Sepharose 4B gels were measured, by using two approaches. In one, binding was measured by a procedure involving equilibration of pure cholinesterase in a small volume of diluted gel slurry (4%, v/v). A partially purified preparation of Electrophorus acetylcholinesterase was included. Pure human cholinesterase bound consistently more tightly to each of the gels than did horse cholinesterase, and the acetylcholinesterase appeared to bind the gels 10-100 times more tightly than did the non-specific cholinesterases. The order of binding for the cholinesterases, beginning with the tightest, was: procainamide-Sepharose 4B, MAC-Sepharose 4B, p-PTA-Sepharose 4B and m-PTA-Sepharose 4B. For the acetylcholinesterase the order was: MAC-Sepharose 4B, procainamide-Sepharose 4B, p-PTA-Sepharose 4B and m-PTA-Sepharose 4B. The second approach involved passing native sera or partially purified sera fractions through 1 ml test columns of each of the four affinity gels to determine their retention capacity for the cholinesterases. With these impure samples, the MAC-Sepharose 4B gels proved superior to the procainamide-Sepharose 4B gels at retaining human cholinesterase, but the opposite was true for the horse cholinesterase.

scholarly journals Effect of temperature and pH on carbamoylation and phosphorylation of serum cholinesterases. Theoretical interpretation of activation energies in complex reactions

1972 ◽  
Vol 130 (2) ◽  
pp. 515-524 ◽  
Author(s):  
V. Simeon ◽  
E. Reiner ◽  
C. A. Vernon
Keyword(s):  
Human Serum ◽  
Rate Constants ◽  
Time Course ◽  
Organophosphorus Compounds ◽  
Horse Serum ◽  
Bimolecular Reaction ◽  
Effect Of Temperature ◽  
Theoretical Interpretation ◽  
Serum Cholinesterase ◽  
Kinetics Of

1. The effect of temperature and pH was studied on the kinetics of inhibition of horse serum and human serum cholinesterase by four organophosphorus compounds and five carbamates. 2. For all compounds, and at each pH and temperature, the inhibition followed the kinetics of a bimolecular reaction with the inhibitor in excess, and with a negligible concentration of the Michaelis complex. 3. The second-order rate constants (ka) for inhibition of human serum cholinesterase by one organophosphate and one carbamate increased from 5° to 40°C with an apparent activation energy of 46kJ/mol (11kcal/mol). 4. The ka constant for inhibition of horse serum cholinesterase increased with temperature from 5° to 30°C, and then decreased from 30° to 40°C. The theoretical interpretation of such an unusual effect of temperature is derived. 5. The increase of ka with pH (human serum cholinesterase) followed the dissociation curve for a single group on the enzyme (pK7.5). 6. Rate constants for decarbamoylation (k+3) were determined, and the time-course of inhibition was calculated from the ka and k+3 constants.

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