The Coagulation of Latex

1946 ◽  
Vol 19 (2) ◽  
pp. 491-493
Author(s):  
William Seifriz
Keyword(s):  
Serum Proteins ◽  
Ph Value ◽  
Particle Surface ◽  
Latex Agglutination ◽  
Electrophoretic Study ◽  
Latex Particles ◽  
Electrophoretic Behavior ◽  
Isoelectric Points ◽  
Buffer Mixture ◽  
Constant Observation

Abstract The mechanism of the coagulation of latex is a very brief chapter in most treatises on rubber. The theories are numerous and conflicting. The most widely accepted interpretation is one in which the destruction of the stabilization membrane is postulated. Recently, in Haiti, I made an electrophoretic study of latex involving the determination of mobility rates and isoelectric points. The timing of the migration of individual latex particles obviously necessitated the use of a microscope. This permitted constant observation of the globules, so that not only were their rate and direction of movement observed, but their aggregation as well. When latex is put into a buffer mixture of a pH value at or near the isoelectric point of the latex, agglutination of the particles takes place. While observing this incipient coagulation of the latex, I was led to the conclusion that, though pH values of isoelectric points indicate a protein covering on latex particles, electrophoretic behavior points to a surface which is, in part, non-protein. The very feeble charge on Cryptostegia latex globules in comparison with the greater charge on Castilloa and the still greater charge on Hevea suggests that there is least protein on the Cryptostegia particles, and most on the Hevea particles. This deduction receives even better support from the complete dissimilarity in the mobility curves of Cryptostegia latex particles and the isolated serum proteins. That there is a nonprotein component of the particle surface is hardly to be doubted. I thought it very probable that this nonionizable component is hydrocarbon, the same which constitutes the core of the latex globule.

An Electrophoretic Study of the Proteins in Rubber Latex Serum

1943 ◽  
Vol 16 (3) ◽  
pp. 542-549
Author(s):  
Charles P. Roe ◽  
Roswell H. Ewart
Keyword(s):  
Serum Proteins ◽  
Total Serum ◽  
Vacuum Sublimation ◽  
Electrophoretic Study ◽  
Stability Behavior ◽  
Illumination System ◽  
Electrophoretic Behavior ◽  
Protein Components ◽  
The Stability ◽  
The Relationship

Abstract 1. The serum from unpreserved rubber (Hevea brasiliensis) latex contains seven electrophoretically distinct protein components. The proteins from whole serum originating in Sumatra and Florida give very similar results in electrophoresis experiments. 2. The relationship between electrophoretic mobility and pH has been determined for five of the seven protein components of unpreserved total latex serum. The results are considerably different from those reported by workers with ammonia-preserved latex, and tend to clarify observed differences in the stability behavior of unpreserved and preserved latex. 3. Ammonia-preservation treatment rapidly alters the electrophoretic behavior of the native protein components of latex serum and reduces the number of resolvable components from seven to two. 4. The preparation of dry latex protein from rubber-free latex serum can be accomplished by the vacuum sublimation of frozen serum. This process does not appear to produce important changes in the electrophoretic properties of the total serum proteins. 5. Minor modifications of the electrodes and of the standard illumination system in the electrophoresis apparatus are described.

scholarly journals A PAPER ELECTROPHORETIC STUDY ON SERUM PROTEINS IN LEAD POISONED RABBITS

Sangyo Igaku ◽  
1959 ◽  
Vol 1 (7-8) ◽  
pp. 678-681
Author(s):  
Yoshio HAYASHI ◽  
Haruo KONDO ◽  
Seinosuke IWAI
Keyword(s):  
Serum Proteins ◽  
Electrophoretic Study

Chemical Depolymerisation of Natural Rubber in Biphasic Medium

2014 ◽  
Vol 1024 ◽  
pp. 193-196
Author(s):  
Ibrahim Suhawati ◽  
Asrul Mustafa
Keyword(s):  
Molecular Weight ◽  
Natural Rubber ◽  
Chemical Structure ◽  
Inner Core ◽  
Particle Surface ◽  
Natural Rubber Latex ◽  
Carbonyl Groups ◽  
Latex Particles ◽  
Liquid Natural Rubber ◽  
Biphasic Medium

The molecular weight of natural rubber (NR) can be reduced via depolymerization reaction to produce liquid natural rubber (LNR) with a molecular weight less than 50 000 g/mol. In the reaction, hydrogen peroxide and sodium nitrite were added to natural rubber latex to initiate a redox type reaction which then breaks the NR chain. Low permeation of reagents into latex particles allows the degradation to occur greater at the latex particle surface relative to the inner core contributes to high molecular weight distribution (MWD) or polydispersity of the LNR obtained. In this recent works, the reaction was carried out in a biphasic medium consisting of water and toluene phases. Toluene swells latex particles as indicated by the SEM micrographs showing changes in the size of latex particles. This occurrence is suggested to increase the influx of reagents into the latex particles. Consequently, with higher permeation of reagents into the latex particles resulted in the decrease of molecular weight and lower polydispersity of the LNR obtained. Chemical structure analysize showed that the LNRs obtained were attached with hydroxyl and carbonyl groups.

Paper electrophoretic study of serum proteins in children with leukemia

1957 ◽  
Vol 51 (3) ◽  
pp. 238-254 ◽  
Author(s):  
Enid F. Gilbert ◽  
E. Clarence Rice ◽  
Krikor O. Gregory
Keyword(s):  
Serum Proteins ◽  
Electrophoretic Study

scholarly journals AN ELECTROPHORETIC STUDY OF IMMUNE SERA AND PURIFIED ANTIBODY PREPARATIONS

1939 ◽  
Vol 69 (1) ◽  
pp. 119-131 ◽  
Author(s):  
Arne Tiselius ◽  
Elvin A. Kabat
Keyword(s):  
High Purity ◽  
Globulin Fraction ◽  
Rabbit Antibody ◽  
Electrophoretic Study ◽  
Serum Component ◽  
Isoelectric Points ◽  
Lower Mobility ◽  
Antibody Preparations

1. Antibody produced in the horse migrates as a new serum component between the ß and γ components, whereas rabbit antibody is electrophoretically identical with the γ globulin component of the serum. 2. In rabbit and monkey antisera the percentage of antibody in the serum and in the γ globulin fraction can be determined by integration of the electrophoresis diagrams of unabsorbed and absorbed sera. Antibody solutions of high purity can be obtained by electrophoretic isolation of the γ globulin of rabbit antisera in which the percentage of antibody to total γ globulin is high. 3. The isoelectric points of pig, cow, horse, and rabbit antibodies have been determined. 4. In horse sera prolonged immunization is accompanied by the formation of another antibody component of lower mobility.

scholarly journals Detection of Anti-Human T-Lymphotropic Virus Type I Antibody in Whole Blood by a Novel Counting Immunoassay

2003 ◽  
Vol 49 (2) ◽  
pp. 275-280 ◽  
Author(s):  
Kazunari Yamaguchi ◽  
Yuji Yonemura ◽  
Hiroaki Okabe ◽  
Yoichi Takahama ◽  
Shinya Nagai ◽  
...  
Keyword(s):  
Virus Type ◽  
Whole Blood ◽  
Blood Cells ◽  
Measuring Method ◽  
Sample Volume ◽  
Latex Agglutination ◽  
Blood Collection ◽  
Type I ◽  
Latex Particles ◽  
T Lymphotropic Virus

Abstract Background: Assays to screen for and confirm the presence of the antibody for human T-lymphotropic virus type I (HTLV-I) are currently performed with serum or plasma. We developed and evaluated a new counting immunoassay (CIA) for the detection of HTLV-I antibody in whole blood, using recombinant and synthetic peptide antigens. Methods: We assessed the CIA for detection of HTLV-I antibody in whole blood and plasma. The CIA is an immunity-measuring method that combines latex agglutination with particle-counting technology. The numbers of agglutinated latex particles, single latex particles, and blood cells in a sample are measured based on differences in particle size between latex particles and blood cells. Results: The CIA and ELISA methods were in agreement for all 24 plasma samples tested, including those from 6 patients with HTLV-I-associated diseases, 6 HTLV-I carriers, and 12 HTLV-I antibody-negative individuals. The concordance between the ELISA (plasma) and the CIA (whole blood) for samples from 24 patients was 100%. The concordance between a particle agglutination method (plasma) and the CIA (plasma or whole blood) for 1065 patients was 99.5%. The concordance between results obtained for 1065 pairs of plasma and whole blood samples with the CIA method was 100%. HTLV-I antibody in whole blood was stable for 3 days after blood collection. With this CIA method, results were available within 15 min. Conclusions: The CIA method can be used in screening for HTLV-I. The use of whole blood rather than serum or plasma reduces the sample volume and number of blood collections required, as well as assay time.

An Electrophoretic Study of the Serum Proteins in Scleroderma

1948 ◽  
Vol 67 (4) ◽  
pp. 504-505 ◽  
Author(s):  
S. A. Walker ◽  
E. P. Benditt
Keyword(s):  
Serum Proteins ◽  
Electrophoretic Study

scholarly journals FACTORS INVOLVED IN THE USE OF ORGANIC SOLVENTS AS PRECIPITATING AND DRYING AGENTS OF IMMUNE SERA

1932 ◽  
Vol 16 (2) ◽  
pp. 243-256 ◽  
Author(s):  
Malcolm H. Merrill ◽  
Moyer S. Fleisher
Keyword(s):  
Organic Solvent ◽  
Organic Solvents ◽  
Serum Proteins ◽  
Ph Value ◽  
Critical Concentration ◽  
Antibody Activity ◽  
Maximum Loss ◽  
High Concentrations ◽  
Lower Temperature ◽  
Complete Precipitation

1. In concentrations of 70 to 75 per cent the organic solvents methyl, ethyl, and propyl alcohols, and acetone cause complete precipitation of serum proteins and produce maximum loss in solubility. We have referred to this concentration range as the critical concentration. 2. As the concentration of the solvents is increased from about 75 per cent precipitation continues complete but loss in solubility progressively decreases until at all concentrations above about 87 per cent the precipitates formed at room temperature are completely soluble. 3. The degree of resolubility of the precipitates formed even in these high concentrations of the organic solvent decreases as the temperature is raised and as the duration of exposure is increased. 4. At 5°C. the precipitates formed in all concentrations of these organic solvents are completely resoluble. Also these solvents exert maximum precipitating effect at lower temperature. 5. Maximum precipitating effect by these organic solvents occurs at about pH 6.0 precipitation becoming progressively less as the pH value is altered either way from this point. 6. The more concentrated the serum, the greater the proportion of protein present that will be precipitated by any given concentrations of organic solvent. 7. A method for preparing dry immune sera has been given. Such dried sera have been extracted with a number of organic compounds without loss in solubility or antibody activity.

scholarly journals CERTAIN EFFECTS OF SALTS ON THE PENETRATION OF BRILLIANT CRESYL BLUE INTO NITELLA

1927 ◽  
Vol 10 (3) ◽  
pp. 425-436 ◽  
Author(s):  
Marian Irwin
Keyword(s):  
Ph Value ◽  
Monovalent Cation ◽  
Borate Buffer ◽  
Brilliant Cresyl Blue ◽  
Rate Of Penetration ◽  
Basic Dye ◽  
Cresyl Blue ◽  
Inhibiting Effect ◽  
Buffer Mixture ◽  
Trivalent Cations

The effect of various substances on living cells may be advantageously studied by exposing them to such substances and observing their subsequent behavior in solutions of a basic dye, brilliant cresyl blue. The rate of penetration of the basic dye, brilliant cresyl blue, is decreased when cells are exposed to salts with monovalent cations before they are placed in the dye solution (made up with borate buffer mixture). This inhibiting effect is assumed to be due to the effect of the salts on the protoplasm. This effect is not readily reversible when cells are transferred to distilled water, but it is removed by salts with bivalent or trivalent cations. In some cases it disappears in dye made up with phosphate buffer mixture, or with borate buffer mixture at the pH value in which the borax predominates, and in the case of NaCl it disappears in dye containing NaCl. No inhibiting effect is seen when cells are exposed to NaCl solution containing MgCl2 before they are placed in the dye solution. The rate of penetration of dye is not decreased when cells are previously exposed to salts with bivalent and trivalent cations. The rate is slightly increased when cells are placed in the dye solution containing a salt with monovalent cation and probably with bivalent or trivalent cations. In the case of the bivalent and trivalent salts the increase is so slight that it may be negligible.

scholarly journals Detection of Rabies Virus Antigen in Dog Saliva Using a Latex Agglutination Test

2000 ◽  
Vol 38 (8) ◽  
pp. 3098-3099 ◽  
Author(s):  
S. Kasempimolporn ◽  
W. Saengseesom ◽  
B. Lumlertdacha ◽  
V. Sitprija
Keyword(s):  
Rabies Virus ◽  
Gamma Globulin ◽  
Fluorescent Antibody ◽  
Antibody Test ◽  
Virus Antigen ◽  
Latex Agglutination ◽  
Agglutination Test ◽  
Glass Slide ◽  
Human Rabies ◽  
Latex Particles

Dog bites are responsible for more than 90% of human rabies deaths in Asia. We developed a simple and inexpensive test based on latex agglutination (LA) for rabies virus antigen detection in dog saliva. Rabies virus antigen could be detected by agglutination on a glass slide using latex particles coated with gamma globulin. By evaluation of paired saliva-brain specimens from 238 dogs, the LA test using saliva was 99% specific and 95% sensitive compared to the fluorescent antibody test (FAT) on brain smears. The advantages of the LA test over the standard FAT are that it is comparatively simple and there is no need to kill the animal before examination.

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