Abstract
Dorsal root ganglion (DRG) neurons from rat and frog were labeled in vitro with [35S]methionine, and the newly synthesized, rapidly transported proteins were collected at ligatures on the sciatic nerves. The proteins were extracted and separated by two-dimensional polyacrylamide gel electrophoresis. Exposure of x-ray film to dried gels allowed comparison of the labeled, rapidly transported proteins from frog and rat. The gel staining patterns of abundant proteins in the sciatic nerves were also compared. Triplets of gels were examined; one gel from frog, one from rat, and one from frog plus rat combined. Among the transported proteins, some (including A2, A17 and/or A18 B6, B14(a-i), C1 C22, and some members of A1(a-i) and B3(a-g)) co-migrated on the gels, suggesting that these proteins have been well conserved during evolution. The gel staining patterns of abundant proteins in the sciatic nerves also show some similarities: two forms of actin, serum albumin, and α- and β-tubulin are each in identical positions on the frog and rat gels. Other sciatic nerve and rapidly transported proteins had similar, but not identical, positions on the gels. A number of the rat and frog proteins had no obvious counterpart. We have calculated the magnitude of expected changes in charge and molecular weight of proteins due to accumulation of point mutations during evolution. We conclude that many of the differences between rat and frog protein patterns on the two-dimensional gels could be the result of such point mutations, but we cannot rule out radical changes in polypeptide sequence of abundance between frog and rat for some of these proteins.
| Original language | English |
|---|---|
| Pages (from-to) | 772-779 |
| Number of pages | 8 |
| Journal | Journal of Neurochemistry |
| Volume | 41 |
| Issue number | 3 |
| State | Published - Jan 1 1983 |
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ASJC Scopus subject areas
- Biochemistry
- Cellular and Molecular Neuroscience
Cite this
Polypeptides in frog and rat : Evolutionary changes in rapidly transported and abundant nerve proteins. / Perry, G. W.; Wilson, D. L.
In: Journal of Neurochemistry, Vol. 41, No. 3, 01.01.1983, p. 772-779.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Polypeptides in frog and rat
T2 - Evolutionary changes in rapidly transported and abundant nerve proteins
AU - Perry, G. W.
AU - Wilson, D. L.
PY - 1983/1/1
Y1 - 1983/1/1
N2 - Dorsal root ganglion (DRG) neurons from rat and frog were labeled in vitro with [35S]methionine, and the newly synthesized, rapidly transported proteins were collected at ligatures on the sciatic nerves. The proteins were extracted and separated by two-dimensional polyacrylamide gel electrophoresis. Exposure of x-ray film to dried gels allowed comparison of the labeled, rapidly transported proteins from frog and rat. The gel staining patterns of abundant proteins in the sciatic nerves were also compared. Triplets of gels were examined; one gel from frog, one from rat, and one from frog plus rat combined. Among the transported proteins, some (including A2, A17 and/or A18 B6, B14(a-i), C1 C22, and some members of A1(a-i) and B3(a-g)) co-migrated on the gels, suggesting that these proteins have been well conserved during evolution. The gel staining patterns of abundant proteins in the sciatic nerves also show some similarities: two forms of actin, serum albumin, and α- and β-tubulin are each in identical positions on the frog and rat gels. Other sciatic nerve and rapidly transported proteins had similar, but not identical, positions on the gels. A number of the rat and frog proteins had no obvious counterpart. We have calculated the magnitude of expected changes in charge and molecular weight of proteins due to accumulation of point mutations during evolution. We conclude that many of the differences between rat and frog protein patterns on the two-dimensional gels could be the result of such point mutations, but we cannot rule out radical changes in polypeptide sequence of abundance between frog and rat for some of these proteins.
AB - Dorsal root ganglion (DRG) neurons from rat and frog were labeled in vitro with [35S]methionine, and the newly synthesized, rapidly transported proteins were collected at ligatures on the sciatic nerves. The proteins were extracted and separated by two-dimensional polyacrylamide gel electrophoresis. Exposure of x-ray film to dried gels allowed comparison of the labeled, rapidly transported proteins from frog and rat. The gel staining patterns of abundant proteins in the sciatic nerves were also compared. Triplets of gels were examined; one gel from frog, one from rat, and one from frog plus rat combined. Among the transported proteins, some (including A2, A17 and/or A18 B6, B14(a-i), C1 C22, and some members of A1(a-i) and B3(a-g)) co-migrated on the gels, suggesting that these proteins have been well conserved during evolution. The gel staining patterns of abundant proteins in the sciatic nerves also show some similarities: two forms of actin, serum albumin, and α- and β-tubulin are each in identical positions on the frog and rat gels. Other sciatic nerve and rapidly transported proteins had similar, but not identical, positions on the gels. A number of the rat and frog proteins had no obvious counterpart. We have calculated the magnitude of expected changes in charge and molecular weight of proteins due to accumulation of point mutations during evolution. We conclude that many of the differences between rat and frog protein patterns on the two-dimensional gels could be the result of such point mutations, but we cannot rule out radical changes in polypeptide sequence of abundance between frog and rat for some of these proteins.
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M3 - Article
C2 - 6603494
AN - SCOPUS:0020502076
VL - 41
SP - 772
EP - 779
JO - Journal of Neurochemistry
JF - Journal of Neurochemistry
SN - 0022-3042
IS - 3
ER -