We describe a mild method for the separation and fractionation of nonhistone chromosomal proteins (NHC proteins) on a preparative scale. Rat liver chromatin is dissociated in 3 M NaCl-10 mM Tris-HCl (pH 8), and is resolved into DNA and protein by gel filtration on Bio-Gel A-50m. The resulting mixture of chromosomal proteins is concentrated by ammonium sulfate precipitation and histones are then removed by cation exchange chromatography on Bio-Rex T J. he histone components of chromatin are now relatively well understood, separated, and even to a considerable degree sequenced (Elgin et al., 1971;Wilhelm et al., 1971). It remains of interest to characterize the nonhistone protein components of chromatin in a similar way. Many approaches to the study of this class of proteins have already been reported (Wang,

ABSTRACIT he metabolism of 13Hj6-benzylamino purine was studied in presenescent and early senescent soybean (Glycine max [L.] Meff.) leaves. In both types of leaves, the metabolism was essentially the same. The principal metabolite was identified as j-(6-benzylaminopurin-9-yl)alanine by mass spectral studies, which included discharge ionization-secondary ion mass spectrometry and pulsed positive ion-negative ion-chemical ionization mass spectrometry. Conversion to this alanine conjugate was found to be inhibited 2,4-dichlorophenoxyacetic acid and 5,7-dichloroindoleacetic acid.