Melanoprotein: absence of a direct melanin-protein relationship in chick embryo melanocytes.
Short-term synthesis of radioactivity labeled melanin (using DL-[2-14C]tyrosine or 2-[2-14C]thiouracil) by chick retinal pigment tissues in vitro was not influenced by inhibitors of protein synthesis, puromycin and cycloheximide. Co-ordinate synthesis of protein is, therefore, unnecessary for melanin synthesis, and melanoproteins must represent secondary interactions between melanin and protein. Melanin was isolated from chick embryo feather germs by extracting the proteins with hot dodecyl sulfate/mercaptoethanol. Melanin isolated from tissues incubated previously in L-[U-14C]valine medium had no associated radioactivity compared to the radioactivity of melanin prepared from tissues incubated in DL-[2-14C]tyrosine or 2-[2-14C]thiouracil. If melanoproteins exist at all, they are non-covalently bonded associations of melanin and melanosomal proteins.
D000818:Animals; D002478:Cells, Cultured; D002642:Chick Embryo; D003513:Cycloheximide / Q000494:pharmacology; D008543:Melanins / Q000378:metabolism*; D008544:Melanocytes / Q000378:metabolism*; D011485:Protein Binding; D011506:Proteins / Q000378:metabolism*; D011691:Puromycin / Q000494:pharmacology; D012160:Retina / Q000378:metabolism; D013889:Thiouracil / Q000378:metabolism
D008543:Melanins; D011506:Proteins; C019464:melanoproteins; D011691:Puromycin; D013889:Thiouracil; D003513:Cycloheximide