| Summary: | A new gel medium for the electrophoretic separation of proteins
was developed and the separation properties were compared with
that of polyacrylamide gel.
The new medium. is based on the combination of Sephadex G-2 5
Superfine and acrylamide (1,4:1) into one separating gel.
It separates certain body fluid proteins into more components
than can be attained with conventional polyacrylamide gel
electrophoresis. This new technique was used to study the
proteins of various animals and the possible influence of
physical exercise, heat exposure and fever on the electrophoretic
properties and concentrations of proteins in the body
fluids of these animals.
Emphasis was laid on albumin since this protein separated into
tv main fractions, an upper and a lower albumin band. These
electrophoretically distinct albumins were of approximate]y
equal concentrations and also cross reacted immunologically.
It was further shown that circulating albumin concentration
may be underestimated by dye binding assays, due to the fact
that the lower albumin fraction does not bind to many dyes.
Limited biochemical analysis suggested that the lower albumin
fraction may be bound to different molecules than the upper
albumin. This differentiation in carrying capacity results
in microheterogeneity of the albumin causing differences in
electrophoretic mobilities.
Possible functional differences of the two albumins were also
studied during physical exercise, heat exposure and fever
conditions. It was found that human subjects not participating
in regular physical exercise had relatively increased lower
albumin concentrations as compared to the same subjects after
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