1887

Abstract

SUMMARY: Clupein at 0·02–0·05% in the liquid nutrient medium used to cultivate nodule bacteria, rapidly killed the bacteria and slowly inactivated a bacteriophage that attacked them. When added to a bacterial culture in liquid medium before adding phage, clupein prevented phage and bacteria from combining; when added after the two had combined, clupein interrupted further stages of phage-host interaction. Clupein at 0·0016% acted bacteriostatically and slowed phage multiplication but did not stop it.

Trypsin and chymotrypsin hydrolyse clupein, trypsin breaking about twice as many peptide bonds as chymotrypsin. At a concentration corresponding to 0·02–0·05% clupein, the peptides produced by chymotrypsin acted bacteriostatically in the liquid nutrient medium; the peptides inactivated phage much more slowly than did intact clupein, and they inhibited phage multiplication by interfering with the combination between phage and host. When added after phage and bacteria had combined, the peptides did not interfere with further stages of phage-host interaction. The smaller peptides produced by trypsin had no effect on host bacteria, phage, or phage/host interaction.

Phage preparations partially inactivated by clupein had their activity partially restored by incubation with trypsin or chymotrypsin.

Clupein, but none of its hydrolytic products, made phage with much non-phage material sedimentable by slow-speed centrifugation.

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/content/journal/micro/10.1099/00221287-14-2-449
1956-04-01
2022-06-29
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References

  1. Bawden F.C., Pirie N.W. 1937; The isolation and some properties of liquid crystalline substances from solanaceous plants infected with three strains of tobacco mosaic virus. Proc. roy. Soc.B 123:274
    [Google Scholar]
  2. Bergmann M. 1942; A classification of proteolytic enzymes. Advanc. Enzymol. 2:49
    [Google Scholar]
  3. Chambers L.A., Henle W. 1941; Precipitation of active influenza A virus from extra-embryonic fluids by protamine. Proc. Soc. exp. Biol., N.Y. 48:481
    [Google Scholar]
  4. Demolon A., Dunez A. 1935; Recherches sur la role du bacteriophage dans la fatigue des luzerniers. Ann. agron., Paris, N.S. 5:89
    [Google Scholar]
  5. Kleczkowski A. 1946; Combination between different proteins and between proteins and yeast nucleic acid. Biochem. J. 40:677
    [Google Scholar]
  6. Kleczkowski J., Kleczkowski A. 1954a; A study of the mechanism of inhibition of bacteriophage multiplication by chymotrypsin. J. gen. Microbiol. 10:285
    [Google Scholar]
  7. Kleczkowski J., Kleczkowski A. 1954b; The effect of ribonuclease on phage- host interaction. J. gen. Microbiol. 11:451
    [Google Scholar]
  8. Kossel A., Dakin H.D. 1904; Über Salmin und Clupein. Z. physiol. Chem. 41:407
    [Google Scholar]
  9. Northrop J.H., Kunitz M., Herriot R.M. 1948; Crystalline Enzymes,. , 2nd ed.. New York: : Columbia University Press;
    [Google Scholar]
  10. Thompson W.H. 1900; Die physiologische Wirkung der Protamine und ihrer Spaltungsprodukte. Z. physiol. Chem. 29:1
    [Google Scholar]
  11. Waldschmidt-leitz E., Kofranyi E. 1935; Über die Struktur der Protamine Strukturaufklarung des Clupeins. Z.physiol. Chem. 236:181
    [Google Scholar]
  12. Waldschmidt-leitz E., Ziegler F., Schäffner A., Weil L. 1931; Über die Struktur der Protamine. I. Protaminase und die Produkte ihrer Einwirkung auf Clupein und Salmin. Z. physiol. Chem. 197:219
    [Google Scholar]
  13. Warren J., Weil M.L., Russ S.B., Jeffries H. 1949; Purification of certain viruses by use of protamine sulfate. Proc. Soc. exp. Biol., N.Y. 72:662
    [Google Scholar]
  14. Warren J., Weil M.L., Russ S.B., Jeffries M. 1950; Applications of protamine precipitation in purification of certain viruses. Fed. Proc. 9:394
    [Google Scholar]
  15. Weber C.J. 1930; A modification of Sakaguchi’s reaction for quantitative determination of arginine. J. biol. Chem. 86: 217
    [Google Scholar]
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