scholarly journals SNAKE BITE PRESENTING AS INTRACRANIAL BLEED WITH NORMAL COAGULATION PARAMETERS

2021 ◽  
pp. 1-2
Author(s):  
Harsh Waingankar ◽  
Prashant Kaushik ◽  
Shruti Sinha ◽  
Jaishree Ghanekar
Keyword(s):  
Phospholipase A2 ◽  
Clinical Laboratory ◽  
Subcutaneous Tissue ◽  
Snake Bite ◽  
Coagulation Profile ◽  
Intracranial Bleed ◽  
Hemorrhagic Risk ◽  
Antibody Complex ◽  
Red Cell Membranes ◽  
Antigen Antibody

Snakebite being commonly encountered emergency in our country and most dreaded one too. It has been estimated that as many as 2.8 million people are bitten by snakes, and 45 900 people die from snakebite every year in India1. The most common coagulopathy associated with snake-bite envenoming is Venom Induced Consumptive Coagulopathy. Venom contain enzymes like proteases, phospholipase A2, hyaluronidase and arginine ester hydrolase. Phospholipase A2 is the factor responsible for hemolysis secondary to the esterlytic effect on the red cell membranes The hyaluronidase causes spread of the venom in the subcutaneous tissue by disrupting mucopolysaccharides. In majority of cases there is disruption in coagulation profile causing increase in PT, INR, aPTT, thrombocytopenia and increase in FDP, which suggests DIC as the probable cause for intracerebral hemorrhage . But always it is not true there are some cases in which there is hemorrhagic risk without alteration in coagulation profile. All my 3 cases present to us with normal coagulation profile , One 26 year old male present within one hour of snake bite and died within 3 days of the bite, while other two presented lately that is 2and 6 day of the snake bite ,of which both survived and had no residual focal deficit at time of discharge. This delayed clinical, laboratory manifestation of vasculotoxic snake due to the delayed seepage of venom from deeper reservoirs in the bite site or due to disassembly of the antigen-antibody complex with reinstitution of circulating unbound venom constituents. Intracranial hemorrhages are poorly understood in case of snake bite and can occur later complication also even after treatment with ASV. Still use of FFP is not advocated in much studies, there is immense need to investigate this area. Use of ASV and FFP without increased WBCT to avoid later complication is to be studied.

Immunofixation electrophoretic techniques applied to identification of proteins in serum and cerebrospinal fluid.

1976 ◽  
Vol 22 (8) ◽  
pp. 1262-1268 ◽  
Author(s):  
L P Cawley ◽  
B J Minard ◽  
W W Tourtellotte ◽  
B I Ma ◽  
C Chelle
Keyword(s):  
Multiple Sclerosis ◽  
Cerebrospinal Fluid ◽  
Clinical Laboratory ◽  
Subacute Sclerosing Panencephalitis ◽  
Coomassie Blue ◽  
Immunofixation Electrophoresis ◽  
Antibody Complex ◽  
Protein Staining ◽  
Monoclonal Proteins ◽  
Antigen Antibody

Abstract We describe the application of immunofixation staining of agarose-gel electrophoretograms in areas where its use in the clinical laboratory is appropriate. Immunofixation electrophoresis consists of an electrophoretic phase followed by a fixation phase in which antiserum is used to precipitate the protein. As long as the antibody is in slight excess or near equivalency, the antigen/antibody complex remains insoluble. The reaction can be detected by visual inspection in indirect light, by protein staining, or by use of antibodies labeled with fluorescein, enzyme, or isotope. In the method described here we primarily have used protein staining (Coomassie Blue) to accentuate the proteins fixed by antisera. All unreacted proteins are removed by pressing with filter paper and saline washing. In the clinical laboratory, this method expedites immunochemical evaluation of samples and may also supplement immunoelectrophoresis. It has been applied successfully in identifying small obscure monoclonal proteins in the serum and cerebrospinal fluid of patients with multiple sclerosis, subacute sclerosing panencephalitis, biclonal gammopathies, serum monoclonal light chains, and mobility shifts of certain proteins, particularly of the complement series. Immunofixation demonstrates that the protein bands present in spinal fluid from multiple sclerosis and subacute sclerosing panencephalitis patients are of the IgG class of immunoglobulins; and non-IgG protein, such as beta and gamma trace proteins, are not detected. We also comment on reverse immunofixation with labeled antigen as a branch of the procedure that allows detection of function of the immunoglobulins separated by electrophoresis.

Visualization of Antibody Transport in Rat Visceral Yolk-Sac Placenta

1982 ◽  
Vol 40 ◽  
pp. 246-247
Author(s):  
William P. Jollie
Keyword(s):  
Phosphate Buffer ◽  
Yolk Sac ◽  
Female Rats ◽  
Thin Sections ◽  
Visceral Yolk Sac ◽  
Antibody Complex ◽  
Cytochemical Reaction ◽  
Hind Foot ◽  
Antigen Antibody ◽  
Yolk Sac Placenta

A technique has been developed for visualizing antibody against horseradish peroxidase (HRP) in rat visceral yolk sac, the placental membrane across which passive immunity previously has been shown to be transferred from mother to young just prior to birth. Female rats were immunized by injecting both hind foot pads with 1 mg HRP emulsified in complete Freund's adjuvant. They were given a booster of 0.5mg HRP in 0.1 ml normal saline i.v. after one week, then bred and autopsied at selected stages of pregnancy, viz., 12, 1 7 and 22 days post coitum, receiving a second booster, injected as above, five days before autopsy. Yolk sacs were removed surgically and fixed immediately in 2% paraformaldehye, 1% glutaraldehye in 0.1 M phosphate buffer with 0.01% CaCl2 at pH 7.4, room temperature, for 3 hr, rinsed 3X in 0.1 M phosphate buffer plus 5% sucrose, then exposed to 1 mg HRP in 1 ml 0.1 M phosphate buffer at pH 7.4 for 1 hr. They were refixed in aldehydes, as above, for 1 5 min (to assure binding of antigen-antibody complex). Following buffer washes, the tissues were incubated in 3 mg diaminobenzidine tetrahydrochloride and 0.01% H2O2 in 0.05 M Tris-HCl buffer for 30 min. After brief buffer washes, they were postfixed in 2% OsO4. in phosphate buffer at pH 7.4, 4°C for 2 hr, dehydrated through a graded series of ethanols, and embedded in Durcupan. Thin sections were observed and photographed without contrast-enhancement with heavy metals. Cytochemical reaction product marked the site of HRP (i.e., antigen) which, in turn, was present only where it was bound with anti-HRP antibody.

INHIBITION OF LIPOLYTIC ACTIVITY OF SYNTHETIC β1–24 AND β1–39 CORTICOTROPHIN BY ANTI-ACTH ANTISERUM

1966 ◽  
Vol 51 (1) ◽  
pp. 88-94 ◽  
Author(s):  
A. Villanueva ◽  
S. J. H. Ashcroft ◽  
J. P. Felber
Keyword(s):  
Guinea Pig ◽  
Lipolytic Activity ◽  
Peptide Hormones ◽  
Fat Pad ◽  
Double Antibody ◽  
Epididymal Fat ◽  
Antibody Complex ◽  
Radio Immunoassay ◽  
Antigen Antibody

ABSTRACT The synthetic ACTH peptides β1–39 and β1–24 stimulated lipolysis as determined by the rat epididymal fat pad in vitro. The stimulating effect of these peptides was diminished by prior incubation of the peptides with antibodies produced by the guinea-pig against ACTH. The stimulating effect of these hormones was also diminished by the double antibody system used in the radio-immunoassay of ACTH and other peptide hormones, in which incubation with antiserum is followed by precipitation of the antigen-antibody complex by rabbit anti-guinea-pig-γ-globulin.

IDENTIFICATION OF LATS AS AN ANTIGEN-ANTIBODY COMPLEX

1973 ◽  
Vol 71 (4_Suppl) ◽  
pp. S11
Author(s):  
K. Schemmel ◽  
L. Weisbecker ◽  
H. Norden ◽  
V. Mokmol ◽  
V. Becker ◽  
...  
Keyword(s):  
Antibody Complex ◽  
Antigen Antibody

scholarly journals Biophysics : Aspects of Amino Acids Sequence in Proteins and Nucleotide Sequence in Nucleic Acids

2013 ◽  
Vol 4 ◽  
pp. 65-74
Author(s):  
Khadka Bahadur Chhetri
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Nucleic Acids ◽  
Polypeptide Chain ◽  
Antibody Complex ◽  
Antigen Antibody

Protein is the polypeptide chain of amino-acid sequence. Proteins of all species, from bacteria to humans, are made up from the same set of 20 standard amino acids. In order to carry out their function they must take a particular shape which is known as fold. All the enzymes hormones and antibodies are also proteins. To treat certain toxic-microorganism or invader we need certain antigen-antibody complex in the organisms. Just as amino-acid sequence forms the proteins, the polynucleotide sequence forms the nucleic acids. The gene is a part of DNA macromolecule responsible for the synthesis of protein chains. There are 20 amino-acids responsible for the formation of protein and 4 nucleotides responsible for the formation of DNA (RNA). Therefore, we can say that protein text is written in 20-letter and the DNA (RNA) text is written in 4-letter language. The information contained in genes in DNA is transferred to mRNA during transcription.The Himalayan Physics Vol. 4, No. 4, 2013 Page: 65-74 Uploaded date: 12/23/2013 

scholarly journals An Interferometric Method of Quantitative Analysis of Antigen-Antibody Reactions in Gels

1957 ◽  
Vol 34 (1) ◽  
pp. 60-70
Author(s):  
G. C. EASTY ◽  
E. J. AMBROSE
Keyword(s):  
Quantitative Analysis ◽  
Interferometric Method ◽  
Interference Fringes ◽  
Diffusion Cells ◽  
Antibody Complex ◽  
Antigen Antibody

1. A sensitive interferometric method of observing antigen-antibody complexes formed by diffusion of the reactants through gels in suitable diffusion cells is described. 2. Bands of antigen-antibody complex, if not too dense, are observed as peaks in the interference fringes, the areas under the peaks being proportional to the quantities present in each band. 3. The method may be made quantitative by measurement of the areas under the peaks of bands in which precipitation has not progressed too far, and by dissolving the bands of dense precipitate by diffusion of a suitable reagent to give peaks in the fringes. 4. An equation expressing the quantity of precipitate present in a band has been derived.

scholarly journals IMMUNOLOGIC STUDIES OF AUTOIMMUNE DISEASE IN NZB/NZW F1 MICE

1969 ◽  
Vol 130 (2) ◽  
pp. 203-216 ◽  
Author(s):  
B. C. Seegal ◽  
L. Accinni ◽  
G. A. Andres ◽  
S. M. Beiser ◽  
C. L. Christian ◽  
...  
Keyword(s):  
Autoimmune Disease ◽  
The Other ◽  
F1 Hybrids ◽  
The Past ◽  
Antibody Complex ◽  
Antigen Antibody

For the past 3 years NZB and NZW mice have been maintained by sister-brother matings from English breeder stock. NZB/NZW F1 hybrids developed lupus-like nephritis during the 6th to 7th month and few survived beyond the 8th month. Renal tissues of these animals were examined with fluorescein-labeled antinucleoside sera, specific for thymine and cytosine, for the presence of denatured DNA in GCW, and with labeled antibody to mouse IgG for the presence of excess host globulin in the same areas. The following results have been obtained: (a) All 51 hybrids, over 5 months of age, had an excess of mouse globulin in GCW. 40 animals between the ages of 5 and 12 months showed, in the same areas, antigens which bound one or both of the antinucleoside antibodies. (b) Renal tissues of 19 NZB mice, 5–19 months old, and 27 NZW mice, 2–18 months old, were examined. Excess host globulin was seen in GCW of 13 NZB and 20 NZW animals. The tissues of only two old NZB mice, 14 months of age, bound antinucleoside antibody but none of the other animals did. The association of rapidly fatal lupus-like nephritis in NZB/NZW F1 mice with denatured DNA and mouse globulin in GCW supports the hypothesis involving this antigen-antibody complex in the pathogenesis of the disease.

Antibody response to immunization with Schistosoma mansoni egg antigen-antibody complex

1963 ◽  
Vol 13 (2) ◽  
pp. 204-210 ◽  
Author(s):  
Walter Stahl ◽  
José Oliver-González ◽  
Amina Rivera de Sala
Keyword(s):  
Antibody Response ◽  
Schistosoma Mansoni ◽  
Antibody Complex ◽  
Antigen Antibody ◽  
Egg Antigen

Purified insulins

1977 ◽  
Vol 15 (5) ◽  
pp. 18-20
Keyword(s):  
Diabetic Complications ◽  
Insulin Requirement ◽  
Insulin Antibodies ◽  
Daily Insulin ◽  
Antibody Complex ◽  
Antigen Antibody ◽  
Immunogenic Properties ◽  
Daily Insulin Requirement

Purified porcine insulins were developed to reduce the immunogenic properties of conventional insulin. About 95% of diabetics who use standard beef insulin develop insulin antibodies within the first 12 weeks of treatment.1 These antibodies may increase the daily insulin requirement and slow the hypoglycaemic action because active insulin may be only gradually released from the antigen-antibody complex. Suggestions that the antibodies also increase the incidence of long-term diabetic complications2–4 are not widely accepted.

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