The N-terminally acetylated form of mammalian histone H1(o), but not that of avian histone H5, increases with age.
We report here on the HPCE separation of two chicken H5 histones, which do not show the heterogeneity (Gln/Arg) at residue 15 first found by Greenaway and Murray [Greenaway and Murray (1971) Nat. New Biol. 229, 233-238]. The two subfractions obtained were identified using reversed-phase HPLC, hydrophilic interaction HPLC, Edman degradation, and MALDI-MS analysis. We found that the two H5 subcomponents differ only by an acetylated (designated H5a) and an unacetylated N-terminus (H5b). In contrast to the N-terminally acetylated form of rat kidney histone H1(o), which increased by about 40% with aging of the animal, the corresponding form of chicken H5 did not: the ratio N-terminally acetylated: unacetylated remained constant (30:70) when histone H5 was extracted from erythrocytes of newly hatched chickens and from adult chickens, respectively. The HPCE technique used in this investigation represents a quick and convenient method for analyzing N-terminally acetylated proteins in the presence of unacetylated forms.
Sarg
B
B
Institute of Medical Chemistry, University of Innsbruck, Fritz Preglstrasse 3, Innsbruck, A-6020, Austria.
Helliger
W
W
Hoertnagl
B
B
Puschendorf
B
B
Lindner
H
H
D000107:Acetylation; D000375:Aging / Q000502:physiology*; D000818:Animals; D002645:Chickens; D002851:Chromatography, High Pressure Liquid; D002918:Chymotrypsin / Q000378:metabolism; D019075:Electrophoresis, Capillary; D004912:Erythrocytes / Q000737:chemistry; D006657:Histones / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D007668:Kidney / Q000737:chemistry / Q000166:cytology; D051381:Rats; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D006657:Histones; D002918:Chymotrypsin