The association of actin with a thyroid lysosomal fraction.
A lysosome-enriched fraction was prepared from bovine thyroid tissue using sucrose gradient centrifugation. An inhibitor of DNAase I was found to co-sediment and co-purify with the lysosomal fraction. This inhibitory activity is blocked by heavy meromyosin in the absence of ATP, and a component of 42000 molecular weight can be isolated by affinity chromatography on DNAase I linked to Sepharose. These results are consistent with the presence of an actin-like protein in a lysosome-enriched preparation from bovine thyroid tissue. Also, an increase in the level of membrane-associated actin is observed in response to thyrotropin stimulation of the thyroid tissue
D000199:Actins / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D003851:Deoxyribonucleases / Q000037:antagonists & inhibitors; D007700:Kinetics; D008247:Lysosomes / Q000187:drug effects / Q000378:metabolism*; D008970:Molecular Weight; D015879:Myosin Subfragments / Q000378:metabolism; D013961:Thyroid Gland / Q000378:metabolism*; D013972:Thyrotropin / Q000494:pharmacology
D000199:Actins; D015879:Myosin Subfragments; D013972:Thyrotropin; D003851:Deoxyribonucleases