SOME OBSERVATIONS ON PROTEIN METABOLISM IN CHROMOSOMES OF NON-DIVIDING CELLS

Author:

Allfrey V. G.1,Daly M. M.1,Mirsky A. E.1

Affiliation:

1. From the Laboratories of The Rockefeller Institute for Medical Research

Abstract

1. The metabolism of chromosomal proteins has been studied in the pancreas, liver, and kidney of adult mice (a) by measuring the rates of glycine-N15 incorporation into histones and residual chromosome fractions, and (b) by measuring the extent to which N15, once incorporated into chromosomal proteins, is retained. 2. The uptake of isotopic nitrogen by these nuclear constituents was compared with that of protein fractions prepared from the cytoplasm by differential centrifugation in sucrose solutions. One such fraction, which comprises the bulk of the ribosenucleoprotein of the cell sediments as a pellet on high speed centrifugation. The supernatant remaining after this centrifugation is a fraction which, in the pancreas, is rich in the secretory enzymes synthesized by the cell. 3. A comparison of the rates of glycine-N15 uptake shows that cytoplasmic ribonucleoprotein is the most active of the protein fractions analyzed. In the pancreas it meets the conditions required of a precursor for the secretory enzymes of the supernate. 4. In all tissues considered the rates of glycine-N15 uptake into histone and residual chromosome fractions are lower, that for histone being the lowest of any of the protein components considered and that for residual protein approximating the over-all rate for cytoplasmic protein. 5. The effects of feeding and fasting upon glycine-N15 incorporation have been studied. In the pancreas, feeding causes a sharp increase in N15 uptake by the mixed tissue proteins and by the nucleoprotein and supernatant protein of the cytoplasm. There is a parallel increase in N15 uptake by the chromosomal constituents—histone and residual protein. 6. A parallelism between N15 uptake in cytoplasmic and chromosomal proteins is also observed in the liver and kidney when over-all protein metabolism is altered by feeding and fasting. 7. The responsiveness of the histones and residual proteins to changes in the environment has also been demonstrated in N15 retention experiments. The loss of isotope once incorporated into chromosomal proteins is much more rapid in fed than in fasted animals.

Publisher

Rockefeller University Press

Subject

Physiology

Cited by 77 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

1. Cytoplasmic and Nuclear Structure in Relation to Metabolic Activities;Ciba Foundation Symposium - Ionizion Radiations and Cell Metabolism;2008-05-30

2. Deoxyribonucleoprotein, A Genetic Material;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22

3. The Chemistry of the Cell Nucleus;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22

4. The synaptonemal complex as part of the nuclear matrix of the flour moth, Ephestia kuehniella;Experimental Cell Research;1984-07

5. Heterogeneity and Territorial Organization of the Nuclear Matrix and Related Structures;International Review of Cytology;1983

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