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J Goudswaard

Publications and source records attributed to J Goudswaard.

52 records · Page 3Linked to original sources
PubMed1977

Selective transport of an oligomeric IgA into canine saliva.

Evidence is presented which shows that an oligomeric IgA myeloma protein possessing J-chain but lacking secretory component, is selectively transferred from serum into canine saliva. The data also demonstrate that 125I-label remains with the IgA during the transfer process. These data interpreted in the light of findings in humans support the concept that the oligomeric form of IgA, devoid of secretory component, is required to achieve selective transport.

Animals↗
PubMed1977

The immunoglobulins of the turkey (Meleagris gallopavo). Isolation and characterization of IgG, IgM and IgA in body fluids, eggs and intraocular tissues.

The distribution of the immunoglobulins IgG, IgM, and IgA in turkey serum, bile, egg white, egg yolk, intestinal secretions, and some intraocular tissues has been studied. Just as in the chicken and the pigeon, IgG is the most abundant immunoglobulin in the serum and IgA in egg white, intestinal secretions and bile. In addition, IgM was detected in serum and egg white, and IgG in egg yolk, iris, vitreous body, and aqueous humor. The discussion deals with the importance of using purified immunoglobulin fractions and heavy-chain-specific antisera in disease studies in the turkey, specially in the case of infectious diseases which lead to the occurrence of "rheumatoid factors".

Animals↗
PubMed1977

Immunochemical determination of human lysozyme by laser nephelometry.

The methods currently available for quantitative determination of lysozyme are based on the capacity of the enzyme to lyse Micrococcus lysodeikticus. Previous attempts to develop immunochemical assays have been reported, but the sensitivity was inferior to that of the most widely used lysoplate method. We describe the development of a sensitive immunochemical method for lysozyme assay in which the recently developed laser nephelometer is used. The sensitivity so achieved is at least comparable to that of the lysoplate method, and in some circumstances better. Results obtained by the lysoplate assay and the nephelometric assay correlate well. Among the advantages of our method are easier handling of larger numbers of samples, quicker results, and the possibility of assaying enzymatically inactive forms of the enzyme.

Animals↗
PubMed1976

Diagnosis of Johne's disease in cattle: a comparison of five serological tests under field conditions.

Sera from 775 adult milking cattle on 13 farms in Friesland and from 359 of the same cattle taken during the following year, were examined for evidence of infection with M johnei by the complement fixation, fluorescent antibody, haemagglutination, haemagglutination-lysis and immunodiffusion tests. Eighteen animals, not clinically affected but which had serologically positive tests were slaughtered and M johnei was isolated in cultures from 16. The fluorescent antibody test was as sensitive as the complement fixation test. The other tests were relatively insensitive and would only be of value as confirmatory tests in the presence of reactions to the first two tests. It is concluded that the use of the fluorescent antibody and the complement fixation test together was of value in detecting sub-clinical Mycobacterium johnei infection.

Animals↗
PubMed1975

Cold hemagglutinin disease in a toy Pinscher dog.

High titers cold agglutinins were demonstrated in the serum of a 7 year old female toy Pinscher with a hemolytic anemia. In vitro, the serum did not show distinct hemolytic properties, but it fixed complement components to both the patient's own red cells and randomly sampled canine erythrocytes and agglutinated these cells at high dilutions at low temperatures (optimally at 0 degrees C). Serum electrophoresis on cellulose acetate membranes failed to reveal a paraproteinemia. Normal canine red cells sensitized with the patient's serum at 0 degrees C and eluted at 40 degrees C, released a cold agglutinin identifiable as IgM by immunoelectrophoresis. Neither IgA nor IgG were detectable in a concentrate of the eluate. The auto-antibody showed no specificity against the canine blood group A antigen and did not react with human O-erythrocytes, irrespective of whether these carried the I- or i-antigens. Following erroneous exposure of the dog to cold, cyanosis and serious gangrene developed at the acra (the ears, nose and feet). In addition, symptoms indicating diffuse intravascular coagulation were observed both hematologically and on pathological-anatomical examination. No primary disease could be demonstrated.

Agglutinins↗
PubMedDate not supplied

The liver in the IgA secretory immune system. Dogs, but not rats and rabbits, are suitable models for human studies.

The liver transport of polymeric IgA (pIgA) from plasma into bile and the immunohistochemical distribution of secretory component (SC) in the liver were studied in dogs, and compared to those in humans, rats, and rabbits. Results were as follows: (i) according to bile and serum protein concentrations and specific activities, plasma pIgA in dogs, like in humans, is transported into bile approximately 10 times more efficiently than albumin, as compared to 320 and 1060 times in rabbits and rats, respectively. (ii) Only approximately 1% of an i.v. dose of [125I]pIgA is transported into bile over 8 hr in dogs, like in humans, as compared to approximately 50% over 3 hr in rats and rabbits. These results agree with much smaller daily fractional catabolic rates of intravascular pIgA in dogs (0.28) and humans (0.48) than in rats (24.0). (iii) Total bile IgA contributes daily about 1.5 mg per kg to intestinal pIgA in dogs, a figure similar in humans (0.8 mg per kg) but much smaller than in rats (38 mg per kg) and rabbits (35 mg per kg). (iv) Biliary obstruction in dogs, like in humans, results only in minor and late increases in serum pIgA levels, contrasting with greater than 8-fold increases within 24 hr in rats and rabbits. (v) Unlike in rats and rabbits, SC in dog liver as well as in human liver cannot be detected in hepatocytes although clearly present in bile duct cells. To conclude: (i) major species differences in plasma-to-bile transport of pIgA exist, most probably related to species differences in the ability of hepatocytes to synthetize SC.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗