ISSN:
0173-0835
Keywords:
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
Lymphoid cells isolated from the spleen of BALB/c nu/nu nude mice were treated with synthetic human thymopoietin, and newly synthesized proteins were labeled by [35S]methionine incorporation. In the control experiment, the same lot of spleen cells were incubated in the labeling medium without the addition of thymopoietin. Urea/detergent-soluble proteins were extracted from the cells after 3 h incubation to be separated by two-dimensional polyacrylamide gel electrophoresis. Spots of [35S]methionine-labeled proteins were visualized by autoradiography and analyzed by image processing. The computer-aided spot matching screened out three major thymopoietin-responsive proteins, TRP-1, -2 and -3. [35S]Methionine incorporation into TRP-3, of which the isoelectric point and molecular mass were approximately pI5 and 10 kDa, respectively, was decreased by the thymopoietin treatment. In contrast with the down regulation, TRP-1, which was slightly higher in pI and slightly larger in molecular mass, and TRP-2, which was slightly higher in pI and almost the same in molecular mass as TRP-3, were evidently induced by the treatment. However, TRPs could not be assigned to Thy-1 antigen on the difference in molecular mass. The specific induction by the thymopoietin treatment suggested that TRP-1 and -2 might be novel proteins related to the intracellular signal transduction.
Additional Material:
2 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/elps.11501501144
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