Antibody production in milk serum of goats experimentally infected with Neisseria gonorrhoeae

1976 ◽  
Vol 22 (8) ◽  
pp. 1113-1119 ◽  
Author(s):  
A. E. Pasieka ◽  
F. E. Ashton ◽  
R. Wallace ◽  
F. Ota ◽  
A. Ryan ◽  
...  
Keyword(s):  
Mammary Gland ◽  
Antibody Response ◽  
Neisseria Gonorrhoeae ◽  
Analytical Ultracentrifugation ◽  
Gel Filtration ◽  
Goat Milk ◽  
Purification And Characterization ◽  
Colony Type ◽  
Milk Serum

Instillation of the goat's mammary gland with Neisseria gonorrhoeae colony type Tl has elicited an antibody response in the goat milk serum (GMS). Purification, and characterization of the GMS by gel filtration, electrophoresis, immunodiffusion, analytical ultracentrifugation. And serological analyses demonstrated that the active immune component was mainly in the IgA and IgG fractions (F2 and F3) of GMS.

Antibody production in goat milk serum after virus instillation of goat mammary gland. V. Biochemical isolation and further characterization of antibodies to various influenza and mumps viruses

1970 ◽  
Vol 16 (12) ◽  
pp. 1153-1159 ◽  
Author(s):  
Arthur E. Pasieka ◽  
L. F. Guerin ◽  
Chas. A. Mitchell
Keyword(s):  
Mammary Gland ◽  
Laboratory Animal ◽  
Goat Milk ◽  
Laboratory Animals ◽  
Lactation Period ◽  
Milk Serum ◽  
Therapeutic Uses ◽  
Biochemical Fractionation ◽  
Specific Inhibitors

This report describes the development of a method for the isolation of antibodies produced in the mammary gland and found in the milk after the instillation and propagation of various myxoviruses. Biochemical fractionation and isolation procedures have been modified and improved over our previous initial reports. The antibodies of the various influenza and mumps viruses that propagated in the gland were found to be associated with lactogammaglobulin. This report also demonstrates that the antibodies produced in the gland and thus given off in the milk are probably the same as those found in the blood if the animal were infected by conventional routes. Purification of the lactoglobulin protein fraction containing the antibody eliminated the non-specific inhibitors. These results were obtained from the various myxoviruses and mumps that propagated in the goat mammary gland.The main advantages of using the mammary gland as compared to using laboratory animals and their blood are as follows.1. Larger volumes of antibodies can be produced at one time (lactation period) against the influenza and mumps viruses for diagnostic and possibly for therapeutic uses.2. The animal (goat) does not appear to be affected whatsoever by the virus instillation and propagation techniques.3. The milk technique is therefore more humane towards laboratory animals. Invariably the laboratory animal does not have to be sacrificed.

Antibody production in goat milk serum after virus instillation of goat mammary gland. VII. Biochemical studies on sham infection with rabies and other non-propagating agents

1975 ◽  
Vol 21 (5) ◽  
pp. 655-661 ◽  
Author(s):  
Arthur E. Pasieka ◽  
L. F. Guerin ◽  
Chas. A. Mitchell
Keyword(s):  
Mammary Gland ◽  
Rabies Virus ◽  
Neutralizing Antibodies ◽  
Analytical Ultracentrifugation ◽  
Sedimentation Coefficient ◽  
Goat Milk ◽  
Neutralizing Antibody ◽  
Antibody Activity ◽  
Gel Chromatography ◽  
Milk Serum

This report describes the development of a method for the production and isolation of neutralizing antibodies against rabies virus (ERA strain) and other agents in the goat mammary gland during active lactation. The rabies virus did not propagate in the gland, but neutralizing antibodies were produced by serial instillations of the antigen. This process was termed 'sham infection.' Antibodies first appeared in the milk about the 20th day and the titer increased until the 28th day. The antibodies were found to be associated with the lactogammaglobulin. The milk globulins were fractionated by gel chromatography and the fraction containing the antibody was isolated. This fraction was further purified and characterized by immunodiffusion, immunoelectrophoresis, and an analytical ultracentrifugation technique. The neutralizing antibody activity after the 29th day was associated with the milk serum IgG fraction. This active fraction was found to have a sedimentation coefficient of 6.8 Svedberg units.

Antibody production in milk serum after antigen instillation of the goat mammary gland. IX. Sham infection studies with Neisseria meningitidis L.C.D.C. 608B

1975 ◽  
Vol 21 (5) ◽  
pp. 662-667 ◽  
Author(s):  
Arthur E. Pasieka ◽  
G. Calver ◽  
C. P. Kenny ◽  
C. Perusse ◽  
L. F. Guerin ◽  
...  
Keyword(s):  
Mammary Gland ◽  
Neisseria Meningitidis ◽  
Large Scale ◽  
Analytical Ultracentrifugation ◽  
Gel Filtration ◽  
Goat Milk ◽  
Scale Production ◽  
Strain Isolation ◽  
Lactating Mammary Gland ◽  
Immune Globulins

Specific immune globulins have been prepared in goat milk in response to the intramammary gland instillation of Neisseria meningitidis 608, serogroup B strain. Isolation, purification, and characterization of the goat whey by gel filtration, electrophoresis, and analytical ultracentrifugation demonstrated that the active immune component resided in the IgA class of globulins, specifically 9.2-S IgA. The potential of the lactating mammary gland as a "biological factory" for the large-scale production of diagnostic antiserum to killed bacterial whole cell antigen is described.

Purification and Characterization of Tissue-Type Plasminogen Activator in Maxillary Mucosa with Chronic Inflammation

1985 ◽  
Vol 54 (02) ◽  
pp. 485-489 ◽  
Author(s):  
Yukiyoshi Hamaguchi ◽  
Masuichi Ohi ◽  
Yasuo Sakakura ◽  
Yasuro Miyoshi
Keyword(s):  
Plasminogen Activator ◽  
Chronic Inflammation ◽  
Gel Filtration ◽  
Potassium Acetate ◽  
Tissue Type ◽  
Purification And Characterization ◽  
Tissue Type Plasminogen Activator ◽  
Urokinase Inhibitor ◽  
Type Plasminogen Activator

SummaryTissue-type plasminogen activator (TPA) was purified from maxillary mucosa with chronic inflammation and compared with urokinase. Purification procedure consisted of the extraction from delipidated mucosa with 0.3M potassium acetate buffer (pH 4.2), 66% saturation of ammonium sulfate, zinc chelate-Sepharose, concanavalin A-Sepharose and Sephadex G-100 gel filtration chromatographies.The molecular weight of the TPA was approximately 58,000 ± 3,000. Its activity was enhanced in the presence of fibrin and was quenched by placental urokinase inhibitor, but not quenched by anti-urokinase antibody. The TPA made no precipitin line against anti-urokinase antibody, while urokinase did.All these findings indicate that the TPA in maxillary mucosa with chronic inflammation is immunologically dissimilar to urokinase and in its affinity for fibrin.

scholarly journals Occurrence of fatty acid epoxide hydrolases in soybean (Glycine max). Purification and characterization of the soluble form

1992 ◽  
Vol 282 (3) ◽  
pp. 711-714 ◽  
Author(s):  
E Blée ◽  
F Schuber
Keyword(s):  
Glycine Max ◽  
Gel Filtration ◽  
Soluble Form ◽  
Soluble Enzyme ◽  
Purification And Characterization ◽  
Epoxide Hydrolases ◽  
Major Activity ◽  
Apparent Homogeneity ◽  
A Minor

Epoxide hydrolases catalysing the hydration of cis-9,10-epoxystearate into threo-9,10-dihydroxystearate have been detected in soybean (Glycine max) seedlings. The major activity was found in the cytosol, a minor fraction being strongly associated with microsomes. The soluble enzyme, which was purified to apparent homogeneity by (NH4)2SO4 fractionation, hydrophobic, DEAE- and gel-filtration chromatographies, has a molecular mass of 64 kDa and a pI of 5.4.

scholarly journals Partial purification and characterization of an endo-α-N-acetylgalactosaminidase from the culture medium of Streptomyces sp. OH-11242

1992 ◽  
Vol 288 (2) ◽  
pp. 475-482 ◽  
Author(s):  
I Ishii-Karakasa ◽  
H Iwase ◽  
K Hotta ◽  
Y Tanaka ◽  
S Omura
Keyword(s):  
Enzyme Activity ◽  
Culture Medium ◽  
Gel Filtration ◽  
Partial Purification ◽  
Gastric Mucus ◽  
Purification And Characterization ◽  
Streptomyces Sp ◽  
Optimum Ph ◽  
New Type

For the purification of a new type of endo-alpha-N-acetylgalactosaminidase from the culture medium of Streptomyces sp. OH-11242 (endo-GalNAc-ase-S) [Iwase, Ishii, Ishihara, Tanaka, Omura & Hotta (1988) Biochem. Biophys. Res. Commun. 151, 422-428], a method for assaying enzyme activity was established. Using purified pig gastric mucus glycoprotein (PGM) as the substrate, oligosaccharides liberated from PGM were pyridylaminated, and the reducing terminal sugars of oligosaccharides larger than Gal beta 1-3GalNAc were analysed by h.p.1.c. The crude enzyme of endo-GalNAc-ase-S was prepared as an 80% (w/v) ammonium sulphate precipitate from the concentrated culture medium. The enzyme was partially purified by gel chromatofocusing and subsequent DEAE-Toyopearl chromatography. Endo-enzyme activity eluted around pI 4.8 on a gel chromatofocusing column and eluted with 0.19-0.25 M-NaCl on a DEAE-Toyopearl column. In the enzyme fraction obtained, no exo-glycosidases or proteases could be detected. The molecular mass of the enzyme was estimated as 105 kDa by gel filtration, and the optimum pH was 5.5. Endo-GalNAc-ase-S hydrolysed the O-glycosidic linkage between GalNAc and Ser (Thr) in 3H-labelled and unlabelled asialofetuin, liberating both the disaccharide (Gal beta 1-3GalNAc) and the tetrasaccharide [Gal beta 1-3 (Gal beta 1-4GlcNAc beta 1-6)GalNAc]. When endo-alpha-N-acetylgalactosaminidase from Alcaligenes sp. (endo-GalNac-ase-A) was incubated with 3H-labelled and unlabelled asialofetuin, only the disaccharide (Gal beta 1-3GalNAc) was liberated.

Purification and characterization of tuberculin-active components from BCG

1975 ◽  
Vol 21 (12) ◽  
pp. 2019-2027
Author(s):  
M. Laguerre ◽  
R. Turcotte
Keyword(s):  
Physicochemical Properties ◽  
Guinea Pigs ◽  
Gel Filtration ◽  
Biologically Active ◽  
Polyacrylamide Gels ◽  
Active Components ◽  
Purification And Characterization ◽  
Molecular Weights ◽  
Antigenic Activity

The tuberculin activity of protoplasmic extracts isolated from living BCG was purified successively by gel filtration on Sephadex G-100 and G-75, and by electrophoresis on 7.5% and on gradient (6–18%) polyacrylamide gels. The tuberculin-active fractions, as determined in BCG-sensitized guinea pigs, were used as the starting material for each of the following fractionation steps.The physicochemical properties and the antigenic activity of the biologically active fractions have shown that a single component, or only a few ones with similar properties, possessed high tuberculin activity. These active components were proteins having relatively high molecular weights (about 72 000) and could behave as antigens.

scholarly journals Purification and Characterization of Endoglucanase from local isolate of Aspergillus flavus

2013 ◽  
Vol 10 (3) ◽  
pp. 844-853
Author(s):  
Baghdad Science Journal
Keyword(s):  
Aspergillus Flavus ◽  
Specific Activity ◽  
Gel Filtration ◽  
Temperature Stability ◽  
Exchange Chromatography ◽  
Purification And Characterization ◽  
Original Activity ◽  
A Value ◽  
Optimum Ph

Endoglucanase produced from Aspergillus flavus was purified by several steps including precipitation with 25 % ammonium sulphate followed by Ion –exchange chromatography, the obtained specific activity was 377.35 U/ mg protein, with a yield of 51.32 % .This step was followed by gel filtration chromatography (Sepharose -6B), when a value of specific activity was 400 U/ mg protein, with a yield of 48 %. Certain properties of this purified enzyme were investigated, the optimum pH of activity was 7 and the pH of its stability was 4.5, while the temperature stability was 40 °C for 60 min. The enzyme retained 100% of its original activity after incubation at 40 °C for 60 min; the optimum temperature for enzyme activity was 40 °C.

Purification and Characterization of Two Proteins from Culture Filtrates of Mycobacterium tuberculosis H 37 Ra Strain

1970 ◽  
Vol 1 (2) ◽  
pp. 164-168
Author(s):  
Thomas M. Daniel ◽  
Lavenia E. Ferguson
Keyword(s):  
Molecular Weight ◽  
Mycobacterium Tuberculosis ◽  
Skin Testing ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Purification And Characterization ◽  
Culture Filtrates ◽  
Zone Electrophoresis

Two proteins have been purified from culture filtrates of Mycobacterium tuberculosis , H 37 Ra strain by a procedure combining gel filtration, diethylaminoethyl (DEAE)-cellulose chromatography, and zone electrophoresis. The two proteins are similar in molecular weight but differ slightly in charge. The faster migrating protein, designated a 1 , is not antigenic. The slower migrating protein, designated a 2 , is antigenic both with respect to antisera and as a skin-testing antigen.

Purification and characterization of a lectin from Xanthomonas campestris NCIM 5028

1996 ◽  
Vol 42 (6) ◽  
pp. 609-612 ◽  
Author(s):  
Bhagyashree Joshi ◽  
Jayant M. Khire ◽  
Hephzibah SivaRaman ◽  
M. Islam Khan
Keyword(s):  
Molecular Mass ◽  
Host Plant ◽  
Xanthomonas Campestris ◽  
Simple Procedure ◽  
Gel Filtration ◽  
Purification And Characterization ◽  
Ammonium Sulphate Precipitation ◽  
Molecular Masses ◽  
Lectin Purification

A lectin was isolated from culture filtrates of Xanthomonas campestris NCIM 5028, by a simple procedure of hydrophobic chromatography on phenyl-Sepharose after ammonium sulphate precipitation. The lectin was a heterodimer, with subunit molecular masses of 30 000 and 28 000. Gel filtration on S-300 column, calibrated with markers, showed its molecular mass to be approximately 70 000. Its isoelectric point was 7.2. The agglutination of the rabbit erythrocytes by the lectin was inhibited by fetuin glycopeptides and host plant (Brassica oleracea) extracts.Key words: Xanthomonas campestris, lectin, purification.

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