12. IMMUNOLOGY OF FISH
477
ancestral gene (cf. Marchalonis and Edelman, 1965; Kabat, 1967a,b;
Putnam, 1969). They also support the idea that the conserved amino acid
positions within the variable portion of L chains may have the function
of acting in the establishment of the general teritary structure of antibodies. Further information on fish Ig has been obtained by Trump
(1968) who used the passive hemagglutination technique to study antibodies for bovine serum albumin produced by goldfish. Two populations
of Ig containing antibodies were obtained and characterized. Both of
these sediment at 16S, and both had a common antigen determinant.
One population was electrophoretically faster than the other and had
a unique second determinant. Whether or not these represent antibody
classes similar to those discussed above is still uncertain, but their occurrence is a good indication of the need for additional comparative
studies on fish antibodies.
This section shows that sufficient studies on the molecular architecture of fish antibodies now exist to verify earlier assumptions that
research on this class will contribute profoundly to the devolpnient of
our understanding of the immunoglobulins, particuarly in view of the
observations reported on the differences between fish and mammalian
7 S antibodies with respect to their relations to homologous ,M, and the
observations of Trump just referred to (see also Uhr et al., 1962).
F. The Specificity of Fish Antibodies
As stated earlier, there is good evidence that fish in general make
phage neutralizing and agglutinating antibodies following antigenic
stimulation. Precipitating antibodies are another story, however. Good
and Papermaster, in 1964, considered the nature of the evolution of
the specificity (avidity) of the antibody combining site. At this time,
only the holostean bowfin and a few other species had been demonstrated to be capable of precipitin production, while several failures
had been reported (cf. also Ridgway et al., 1966).
The successful cases had not been pursued in depth, and one of them
(Sirotinin, 1959) even led to the conclusion that fish antibody against
the serum of other species reacted indiscriminately with heterologous
antigen. This stimulated Everhart and Shefner (1966) to a further investigation of the specificity of goldfish antibodies, using bovine serum
(BSA) as homologous antigen. The serum albumins of the human,
sheep, and horse were used as heterologous antigen, with rabbit antiBSA as a comparative control. The standard quantitative precipitin
test was used to determine equivalence points and cross-reactivity. In
477
ancestral gene (cf. Marchalonis and Edelman, 1965; Kabat, 1967a,b;
Putnam, 1969). They also support the idea that the conserved amino acid
positions within the variable portion of L chains may have the function
of acting in the establishment of the general teritary structure of antibodies. Further information on fish Ig has been obtained by Trump
(1968) who used the passive hemagglutination technique to study antibodies for bovine serum albumin produced by goldfish. Two populations
of Ig containing antibodies were obtained and characterized. Both of
these sediment at 16S, and both had a common antigen determinant.
One population was electrophoretically faster than the other and had
a unique second determinant. Whether or not these represent antibody
classes similar to those discussed above is still uncertain, but their occurrence is a good indication of the need for additional comparative
studies on fish antibodies.
This section shows that sufficient studies on the molecular architecture of fish antibodies now exist to verify earlier assumptions that
research on this class will contribute profoundly to the devolpnient of
our understanding of the immunoglobulins, particuarly in view of the
observations reported on the differences between fish and mammalian
7 S antibodies with respect to their relations to homologous ,M, and the
observations of Trump just referred to (see also Uhr et al., 1962).
F. The Specificity of Fish Antibodies
As stated earlier, there is good evidence that fish in general make
phage neutralizing and agglutinating antibodies following antigenic
stimulation. Precipitating antibodies are another story, however. Good
and Papermaster, in 1964, considered the nature of the evolution of
the specificity (avidity) of the antibody combining site. At this time,
only the holostean bowfin and a few other species had been demonstrated to be capable of precipitin production, while several failures
had been reported (cf. also Ridgway et al., 1966).
The successful cases had not been pursued in depth, and one of them
(Sirotinin, 1959) even led to the conclusion that fish antibody against
the serum of other species reacted indiscriminately with heterologous
antigen. This stimulated Everhart and Shefner (1966) to a further investigation of the specificity of goldfish antibodies, using bovine serum
(BSA) as homologous antigen. The serum albumins of the human,
sheep, and horse were used as heterologous antigen, with rabbit antiBSA as a comparative control. The standard quantitative precipitin
test was used to determine equivalence points and cross-reactivity. In