The Separation of Proteins Based on Their Age, for the Study of Protein Degradation in Escherichia coli

References

1. Achstetter T., Ehman C., Wolf D.H. 1981; New proteolytic enzymes in yeast. Archives of Biochemistry and Biophysics 207:445–454
   [Google Scholar]
2. Aloyo V. 1979; Scintillation counting of ³H and ¹⁴C- containing gel slices: a one-step method. Analytical Biochemistry 99:161–164
   [Google Scholar]
3. Arias I.M., Doyle D., Schimke R.T. 1969; Studies on the synthesis and degradation of the proteins of the endoplasmic reticulum of rat liver. Journal of Biological Chemistry 244:3303–3315
   [Google Scholar]
4. Bond J.S. 1975 In Intracellular Protein Turnover pp. 281–294 Schimke R.T., Katunuma N. Edited by New York:: Academic Press.;
   [Google Scholar]
5. Boudet A., Humphrey T.J., Davies D.D. 1975; The measurement of protein turnover by density labelling. Biochemical Journal 152:409–416
   [Google Scholar]
6. Brinster R.L., Brunster S., Joseph X., Levey I.L. 1979; Protein degradation in the mouse blastocyst. Journal of Biological Chemistry 254:1927–1931
   [Google Scholar]
7. Calandruccio J.H., Larrabee A.R. 1981; Protein turnover in chemostat cultures of Escherichia coli. Archives of Biochemistry and Biophysics 210:270–274
   [Google Scholar]
8. Cooke R.J., Oliver J., Davies D.D. 1980; General characteristics of normal and stress enhanced protein degradation in Lemna minor. Biochemical Journal 192:499–506
   [Google Scholar]
9. Davies D.D. 1980; The measurement of protein turnover in plants. Advances in Botanical Research 8:65–126
   [Google Scholar]
10. Dice J.F., Goldberg A.L. 1975a; A statistical analysis of the relationship between degradative rates and molecular weights of proteins. Archives of Biochemistry and Biophysics 170:213–219
    [Google Scholar]
11. Dice J.F., Goldberg A.L. 1975b; Relationship between in vivodegradative rates and isoelectric points of proteins. Proceedings of the National Academy of Sciences of the United States of America 72:3893–3897
    [Google Scholar]
12. Dice J.F., Walker C.D., Byrne B., Cardill A. 1978; General characteristics of protein degradation in diabetes and starvation. Proceedings of the National Academy of Sciences of the United States of America 75:2093–2097
    [Google Scholar]
13. Dice J.F., Hess E.J., Goldberg A.L. 1979; Studies on the relationship between the degradative rates of proteins in vivo and their isoelectric points. Biochemical Journal 178:305–312
    [Google Scholar]
14. Duncan W.E., Offerman M.K., Bond J.S. 1980; Intracellular turnover of stable and labile soluble liver proteins. Archives of Biochemistry and Biophysics 199:331–341
    [Google Scholar]
15. Garlick P.J., Waterlow J.C., Swick R.W. 1976; Measurement of protein turnover in rat liver. Biochemical Journal 156:657–663
    [Google Scholar]
16. Goldberg A.L., Dice J.F. 1974; Intracellular protein degradation in mammalian and bacterial cells. Annual Review of Biochemistry 43:835–869
    [Google Scholar]
17. Goldberg A.L., St John A.C. 1976; Intracellular protein degradation in mammalian and bacterial cells. Part II. Annual Review of Biochemistry 45:835–869
    [Google Scholar]
18. Gustafson G., Ryan C.A. 1976; Specificity of protein turnover in tomato leaves. Accumulation of proteinase inhibitors induced with the wound hormone PIIF. Journal of Biological Chemistry 251:7004–7110
    [Google Scholar]
19. Holzer H., Heinrich P.C. 1980; Control of proteolysis. Annual Review of Biochemistry 49:63–71
    [Google Scholar]
20. Hopgood M.F., Ballard F.J. 1974; The relative stability of liver cytosol enzymes incubated in vitro. Biochemical Journal 144:371–376
    [Google Scholar]
21. Horst M.N., Roberts R.M. 1979; Analysis of polypeptide turnover rates in Chinese hamster ovary cell plasma membranes using two dimensional electrophoresis. Journal of Biological Chemistry 254:5000–5007
    [Google Scholar]
22. Johnson R.W., Kenny F.T. 1973; Regulation of tyrosine aminotransferase in rat liver. Journal of Biological Chemistry 248:4528–4531
    [Google Scholar]
23. Kemshead J.T., Hipkiss A.R. 1976; Degradation of abnormal proteins in Escherichia coli. European Journal of Biochemistry 77:185–192
    [Google Scholar]
24. Kuehl L., Sumsion E. 1970; Turnover of several glycolytic enzymes. Journal of Biological Chemistry 245:6616–6623
    [Google Scholar]
25. Larrabee K.L., Phillips J.O., Williams G.J., Larrabee A.R. 1980; The relative rates of protein synthesis and degradation in a growing culture of Escherichia coli. Journal of Biological Chemistry 255:4125–4130
    [Google Scholar]
26. Malano J., Gancedo C. 1974; Specific inactivation of fructose-1,6-biphosphatase from Saccharomyces cerevisiae by a yeast protease. European Journal of Biochemistry 44:213–217
    [Google Scholar]
27. Mandelstam J. 1957; Turnover of proteins in growing and non-growing populations of Escherichia coli. Biochemical Journal 67:110–119
    [Google Scholar]
28. Mandelstam J. 1960; The intracellular turnover of proteins and nucleic acids and its role in biochemical differentiation. Bacteriological Reviews 24:289–308
    [Google Scholar]
29. Mann D.F., Shah K. 1979; Correlation of rat liver enzyme half-life with retention in detergent affinity columns. Federation Proceedings 38:414
    [Google Scholar]
30. Mclendon G., Radany E. 1978; Is protein turnover thermodynamically controlled?. Journal of Biological Chemistry 253:6335–6337
    [Google Scholar]
31. Mclendon G., Smith M. 1978; Equilibrium and kinetic studies of unfolding of homologous cytochromes c. Journal of Biological Chemistry 253:4004–4008
    [Google Scholar]
32. Mosteller R.D., Goldstein R.V., Nishimoto K.R. 1980; Metabolism of individual proteins in exponentially growing Escherichia coli. Journal of Biological Chemistry 255:2524–2532
    [Google Scholar]
33. Neiman R.H., Paulsen L.L. 1963; Spectrophotometric estimation of nucleic acid of plant leaves. Plant Physiology 38:31–35
    [Google Scholar]
34. Penke B., Ferenci R., Kovacs K. 1974; A new acid hydrolysis method for determining tryptophan in peptides and proteins. Analytical Biochemistry 60:45–50
    [Google Scholar]
35. Pine M.J. 1972; Turnover of intracellular proteins. Annual Review of Microbiology 26:103–126
    [Google Scholar]
36. Poole B. 1971; The kinetics of disappearance of labelledleucine from the free leucine pool of rat liver and its effect on the apparent turnover of catalase and other hepatic proteins. Journal of Biological Chemistry 246:6587–6591
    [Google Scholar]
37. Richards L., Thurston C.F. 1980; Protein turnover in Chlorella fusca var.vacuolata: measurement of the overall rate of intracellular protein degradation using isotope exchange with water. Journal of General Microbiology 121:49–61
    [Google Scholar]
38. Roberts J.W., Roberts C.W., Craig N.L. 1978; Escherichia coli recA gene product inactivates phage λ repressor. Proceedings of the National Academy of Sciences of the United States of America 75:4714–4718
    [Google Scholar]
39. Roberts R.M., Yuan B.O.-C. 1975; Radio labelling of mammalian cells in tissue culture by use of acetic anhydride. Archives of Biochemistry and Biophysics 171:226–233
    [Google Scholar]
40. Robinson A.B., Rudd C.J. 1974; Deamidation of glutaminyl and asparaginyl residues in peptides and. Proceedings of the National Academy of Sciences of the United States of America 71:885–888
    [Google Scholar]
41. Robinson A.B., Rudd C.J. 1974; Deamidation of glutaminyl and asparaginyl residues in pepyides and proteins. Current Topics in Cellular Regulation 8:247–298
    [Google Scholar]
42. Russell S.M., Burgess R.J., Mayer R.J. 1980; Protein degradation in rat liver during post-natal development. Biochemical Journal 192:321–330
    [Google Scholar]
43. Steinert P.M., Balige B.S., Munro H.N. 1974; Available sulphydryl groups of mammalian ribosomes in different functional states. Journal of Molecular Biology 88:895–911
    [Google Scholar]
44. St John A., Jakabusi K., Bevin D. 1979; Degradation of proteins in steady-state cultures of Escherichia coli. Biochimica et biophysica acta 586:537–544
    [Google Scholar]
45. Tsurugi K., Morita T., Ogata K. 1974; Mode of degradation of ribosomes in regenerating rat liver in vivo. European Journal of Biochemistry 45:119–125
    [Google Scholar]
46. Tweto J., Doyle D. 1976; Turnover of the plasma membrane proteins of hepatoma tissue culture cells. Journal of Biological Chemistry 251:872–882
    [Google Scholar]
47. Varandari P.T., Shroyer L.A. 1973; Insulin degradation. Biochimica et biophysica acta 295:630–636
    [Google Scholar]
48. Walker J.H., Burgess R.J., Mayer R.J. 1978; Relative rates of turnover of subunits of mitochondrial proteins. Biochemical Journal 176:927–932
    [Google Scholar]
49. Weber K., Pingle J.R., Osborn H. 1972; Measurement of molecular weights by electrophoresis on SDS acrylamide gels. Methods in Enzymology 26:3–27
    [Google Scholar]
50. Weismeyer H., Cohn M. 1960; The characterization of the pathway of maltose utilization by Escherichia coli. Biochimica et biophysica acta 39:417–428
    [Google Scholar]
51. Wilde C.J., Paskin N., Saxton J., Mayer R.J. 1980; Protein degradation during terminal cyto-differentiation. Biochemical Journal 192:311–320
    [Google Scholar]
52. Willetts N.S. 1967; Intracellular protein breakdown in non-growing cells of Escherichia coli. Biochemical Journal 103:453–464
    [Google Scholar]
53. Wolf D.H. 1982; Protein action in vitro versusproteinase function in vivo: mutants shed light on intracellular proteolysis in yeast. Trends in Biochemical Science 7:35–37
    [Google Scholar]
54. Zak R., Martin A.F., Prior G., Rabinowitz M. 1977; Comparison of turnover of several myofibrillar proteins and critical evaluation of the double isotope method. Journal of Biological Chemistry 252:3430–3435
    [Google Scholar]
55. Zak R., Martin A.F., Blough R. 1979; Assessment of protein turnover by use of radioisotopic tracers. Physiological Reviews 59:407–447
    [Google Scholar]