Microheterogeneity of rat α?-fetoprotein, immunochemical properties
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概要
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A purified and homogeneous preparation of rat α?-fetoprotein ( α?-FP), as judged by both electrophoresis on Cellogel and immuno-electrophoresis, were separated into two components, namely a α?a and α?b-FP, by disc electrophoresis on 7% polyacrylamide gel. These two components had definite differences in electrostatic net charge and gave only a single band on SDS-disc electrophoresis. Immunological reactivity or electrophoretic separation or mobility thereof could be altered by treatment with either sulfhydryl inhibi-tors or reducting agents but not by treatment with protein denat-urants. Electrophoresis of neuraminidase-treated α?-FP on 5% polyacrylamide gel yielded clearly separable, slower moving com-ponents, first four to six and finally two components depending on the time of incubation with neuraminidase. The time-dependent conversion of faster into slower migrating components of both α?a-FP (RBPB 0.88→0.85→0.83) and α?b-FP (RBPB 0.85→0.80→0.78→0.76) upon neuraminidase treatment was confirmed by re-electrophoresis of separated and similarly treated α?a and α?b-FP. Both α?a and 1b-FP treated with and without neuraminidase gave a single fused precipitin line against the antiserum in Ouchterlony double-diffusion analysis. On the basis of the changes in electrophoretic mobilities of these intermediates, α?a and α?b-FP were estimated to have at least 2.5 and 4.5 molecules of sialic acid per molecule, respectively. The nature of additional negative charges required for α?a-FP to move faster than α?b-FP at an alkaline pH is discussed.
- 札幌医科大学の論文
- 1974-03-30
札幌医科大学 | 論文
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