The primary structure of two polypeptide chains from preparations of homeostatic thymus hormone (HTH alpha and HTH beta) entire-chain identities to two histones.
The primary structures of the 2 polypeptide chains (HTH alpha and HTH beta) of the homeostatic thymus hormone (HTH) were determined. The entire structures were found to be identical to those of histones H2A and H2B, respectively, without evidence for sub-types, proteolytic processings, or other peptide fragments. The results show that suggestions for new extranuclear and hormone-like histone functions apply to HTH preparations with intact protein chains of the H2 histones.
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003488:Cyanogen Bromide; D010450:Endopeptidases; D006657:Histones; D010446:Peptide Fragments; D013950:Thymus Gland / Q000032:analysis*; D014357:Trypsin
D006657:Histones; D010446:Peptide Fragments; D010450:Endopeptidases; D014357:Trypsin; C042769:Staphylococcus aureus glutamic protease; D003488:Cyanogen Bromide