Clinical Biochemistry of Domestic Animals (Sixth Edition) - UMK ...

V. Methodology
127
Although attempts have been made to classify the
serum protein peaks in an electrophoretogram into more
fractions ( Keay, 1982 ; Keay and Doxey, 1982 ), it is the
division into albumin, α 1 -, α 2 -, β 1 -, β 2 -, γ 1 -, and γ 2 -globulin
fractions ( Trumel et al. , 1996 ) that is predominantly used
in the diagnosis of the dysproteinemias (Section VII.B).
Agarose gel electrophoresis can therefore separate serum
protein into several fractions, but apart from albumin,
each of these is composed of a number of different proteins.
This produces a frustrating limit to the usefulness
of SPE in disease diagnosis. More advanced methods of
protein separation have been developed but are not at present
practical for a routine clinical biochemistry laboratory
because of cost, reproducibility, and the ability to analyze
the amount of data that can be generated. However, if these
obstacles could be overcome, protein separation would
become even more useful than at present.
A recently introduced modification to the commercially
available agarose gel allows high-resolution electrophoresis
(HRE) to be employed for SPE. This method has been
applied to canine serum and was able to localize specific
serum proteins within the different subfractions. Thus,
haptoglobin and α 2 -macroglobulin were identified in the
α 2 fraction, β -lipoprotein and complement C3 were located
in the β 1 region, and transferrin and IgM were located in
the β 2 region ( Abate et al. , 2000 ). The use of HRE may
become more widespread as it is as user-friendly as conventional
agarose electrophoresis.
Pig
Albumin
Sheep FIGURE 5-3 Electrophoretogram of
agarose gel serum protein electrophoresis
of serum from healthy
Albumin
animals.
α 1
β
α
α 2 γ
2 γ
β
α 1
Cow
Dog
Albumin
Albumin
α 1 α 2
β
γ
α 1
α 2
β 1
β 2
γ
Cat
Horse
Albumin
Albumin
α 1
α 2
β 1 β2 γ
α 1
α 2
β 1
β 2
γ