Effect of thyrotropin on the phosphorylation of thyroid chromosomal proteins.
Thyrotropin (TSH) stimulated the phosphorylation of histone H1 in calf thyroid slices but had no effect on other classes of histones. Phosphorylation of total phenol-soluble nonhistone chromosomal proteins was not affected by incubation with TSH. However, when these phenol-soluble nonhistone chromosomal proteins were analysed by two-dimensional gels involving isoelectrofocusing and dodecyl sulfate-polyacrylamide gel electrophoresis, TSH was shown to stimulate the phosphorylation of two specific groups of phosphoproteins with molecular weights between 35,000 and 45,000 and isoelectric points at pH values of 5.4-6.0. This increase in phosphorylation with TSH stimulation was confirmed by quantitative analysis of one-dimensional isoelectrofocusing gels.
D000818:Animals; D002417:Cattle; D002868:Chromosomal Proteins, Non-Histone / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D006657:Histones / Q000378:metabolism*; D066298:In Vitro Techniques; D007525:Isoelectric Focusing; D010766:Phosphorylation; D013961:Thyroid Gland / Q000378:metabolism* / Q000648:ultrastructure; D013972:Thyrotropin / Q000494:pharmacology*
D002868:Chromosomal Proteins, Non-Histone; D006657:Histones; D013972:Thyrotropin