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ELECTROPHORETIC CHARACTERIZATION OF LEUCINE‐, GLUCOSAMINE‐ AND FUCOSE‐LABELLED PROTEINS RAPIDLY TRANSPORTED IN FROG SCIATIC NERVE
Author(s) -
Edström A.,
Mattsson H.
Publication year - 1973
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1973.tb06033.x
Subject(s) - fucose , glucosamine , leucine , biochemistry , cycloheximide , molecular mass , chemistry , gel electrophoresis , sciatic nerve , electrophoresis , glycoprotein , biology , protein biosynthesis , amino acid , anatomy , enzyme
—[ 3 H]Leucine, [ 3 H]glucosamine and [ 3 H]fucose were incorporated in vitro into proteins in frog sciatic ganglia and subsequently transported at a rapid rate along the sciatic nerve towards a ligature, in front of which they accumulated. The synthesis of transported fucose‐labelled proteins is closely linked to protein synthesis but is not dependent on RNA synthesis, as judged by effects after incubation for 17 h in the presence of cycloheximide and actinomycin D. Labelled ganglionic as well as transported material were solubilized in sodium dodecyl sulphate and characterized by polyacrylamide gel electrophoresis. The bulk of ganglionic proteins, labelled with any of the precursors used, had molecular weights exceeding 40,000. The radioactivity patterns of leucine‐ and glucosamine‐labelled ganglionic proteins showed similarities with dominant peaks corresponding to molecular weights of about 75,000 and 50,000. The last peak was almost lacking in fucose‐labelled ganglionic components. Leucine‐ and glucosamine labelled‐transported proteins exhibited characteristic and similar electrophoretic distributions in contrast to the pattern of fucose‐labelled nerve proteins, which was more polydisperse. The most conspicious nerve proteins corresponded to molecular weights of about 75,000 and 18,000. There was a remarkable agreement in the profile of leucine‐labelled transported nerve proteins and fucose‐labelled ganglionic proteins. In the light of these observations the possibility that glycoproteins constitute a large part of rapidly transported proteins will be discussed.