The Rate of Formation of Hyaluronidase, Coaǵulase and Total Extracellular Protein by Strains of Free

Abstract

SUMMARY: Hyaluronidase is formed as a constitutive enzyme by growing in either broth or casein hydrolysate media. The lag in the appearance of hyaluronidase activity after inoculation of a culture is longer than the lag in growth. A change in the rate of formation of hyaluronidase therefore occurs after exponential growth has been established. Activity per unit volume of culture supernatant increases exponentially faster after this initial lag than the mass of bacteria; it stops increasing abruptly sooner than growth. Coagulase appears, after inoculation, without lag additional to that in growth but increases at a slower rate than growth until it too ceases to increase before growth stops. Evidence is presented to show that changes in enzymic activity of the culture represent enzyme formation and not secondary changes in formed protein or secretion phenomena. The changes in rate of enzyme formation are connected with processes controlling enzymic specificity of the proteins rather than with general processes involved in manufacturing extracellular protein.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-10-2-209
1954-04-01
2024-03-29
Loading full text...

Full text loading...

/deliver/fulltext/micro/10/2/mic-10-2-209.html?itemId=/content/journal/micro/10.1099/00221287-10-2-209&mimeType=html&fmt=ahah

References

  1. Anderson P. A. 1953; Automatic recording of the growth rates of continuously cultured micro-organisms. J. gen. Physiol 36:733
    [Google Scholar]
  2. Curran H. R., Evans F. R. 1942; The killing of bacterial spores in fluids by agitation with small inert particles. J. Bact 43:125
    [Google Scholar]
  3. Davies G. E. 1951; Factors influencing the in vitro production of staphylococcal coagulase. J. gen. Microbiol 5:687
    [Google Scholar]
  4. Fischer A. 1935; Gerinnungszeit und Konzentration des Gerinnungsstoffes. Bioche. Z 278:320
    [Google Scholar]
  5. Gale E. F. 1943; Factors influencing the enzymic activities of bacteria. Bact. Rev 7:139
    [Google Scholar]
  6. Gale E. F. 1946; The bacterial amino acid decarboxylases. Advanc. Enzymol 6:1
    [Google Scholar]
  7. Gale E. F. 1951 In Bacterial Physiology p. 436 Werkman G. H., Wilson P. by Academic Press Inc;
    [Google Scholar]
  8. Jeener B. 1953; Ribonucleic acid and protein synthesis in continuous cultures of Polytomella caeca. Arch. Bioche 43:831
    [Google Scholar]
  9. Lowry O. H., Rosebrough N. J., Farr A. Z., Randall R. J. 1951; Protein measurement with the Folin phenol reagent. J. biol. Chem 193:265
    [Google Scholar]
  10. Meyer K., Rapport M. M. 1951; The inhibition of testicular hyaluronidase by heavy metals. J. biol. Chem 188:485
    [Google Scholar]
  11. Monod J. 1950; The technique, theory and application of continuous culture. Ann. Inst. Pasteur 79:390
    [Google Scholar]
  12. Novice A., Szilard L. 1950; Experiments with the chemostat on spontaneous mutations of bacteria. Proc. nat. Acad. Sci., Wash 36:708
    [Google Scholar]
  13. Rogers H. J. 1945; Conditions controlling the production of hyaluronidase by micro-organisms grown in simplified media. Bioche. J 39:435
    [Google Scholar]
  14. Rogers H. J. 1953; Variant populations within a hyaluronidase producing culture of Staphylococcus aureus. J. Path. Bact 66:545
    [Google Scholar]
  15. Tolksdoref S., McCready M. H., McCullagh D. R., Schwenk E. 1949; The turbidimetric assay of hyaluronidase. J. Lab. clin. Med 34:74
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-10-2-209
Loading
/content/journal/micro/10.1099/00221287-10-2-209
Loading

Data & Media loading...

Most cited Most Cited RSS feed