1887

Abstract

Two inducible polygalacturonases (PG-1 and PG-2) from culture filtrates of were purified to homogeneity by CM-cellulose chromatography and isoelectric focusing in a narrow pH range (pH 6 to 8). They were both hydrolytic enzymes classifiable as endopolygalacturonases [poly(1,4---galacturonide) glycanohydrolase; EC 3.2.1.15]. PG-1 and PG-2, focusing at pH 6·41 and 6·57 respectively, each consisted of a single polypeptide chain having an apparent molecular weight of 32000 as determined by gel filtration on Sephadex G-100; they were both glycoproteins and had carbohydrate contents of 0·033 and 0·062 mg sugar (mg protein) respectively. When the isoenzymes were incubated with different plant tissues, they were not absorbed by any of them.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-104-2-305
1978-02-01
2021-10-16
Loading full text...

Full text loading...

/deliver/fulltext/micro/104/2/mic-104-2-305.html?itemId=/content/journal/micro/10.1099/00221287-104-2-305&mimeType=html&fmt=ahah

References

  1. Andrews P. 1965; The gel filtration behaviour of proteins related to their molecular weight over a wide range. Biochemical Journal 91:595–606
    [Google Scholar]
  2. Bateman D. F. 1972; The polygalacturonase complex produced by Sclerotium rolfsii. Physiological Plant Pathology 2:175–184
    [Google Scholar]
  3. Bateman D. F., Millar R. L. 1966; Pectic enzymes in tissue degradation. Annual Review of Phytopathology 4:119–146
    [Google Scholar]
  4. Cervone F., Scala A., Scala F. 1977a; Polygalacturonase from Rhizoctonia fragariae. Further characterization of two isoenzymes and their action towards strawberry tissues. Physiological Plant Pathology in the Press
    [Google Scholar]
  5. Cervone F., Scala A., Foresti M., Cacace M. G., Noviello C. 1977b; Endopolygalacturonase from Rhizoctonia fragariae. Purification and characterization of two isoenzymes. Biochimica et biophysica acta 482:379–385
    [Google Scholar]
  6. Fanelli C., Cervone F. 1977; Polygalacturonase and cellulase production by Trichoderma koningii and Trichoderma pseudokoningii. Transactions of the British Mycological Society 68:291–294
    [Google Scholar]
  7. Laemmli U. K. 1970; Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, London 227:680–685
    [Google Scholar]
  8. Lowry O. H., Rosebrough N. J., Farjr A. L., Randall R. J. 1951; Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193:265–275
    [Google Scholar]
  9. Miller G. L. 1959; Use of dinitrosalicylic acid reagent for determination of reducing sugar. Analytical Chemistry 31:426–427
    [Google Scholar]
  10. Mussel H. W., Strouse B. 1972; Characterization of two polygalacturonases produced by Verticillium albo-atrum. Canadian Journal of Biochemistry 50:625–632
    [Google Scholar]
  11. Nasuno S., Starr M. P. 1966; Polygalacturonase of Erwinia carotovora. Journal of Biological Chemistry 241:5298–5306
    [Google Scholar]
  12. Spiro R. G. 1966; Analysis of sugars found in glycoproteins. Methods in Enzymology 8:3–26
    [Google Scholar]
  13. Strand L. L., Corden M. E., Macdonald D. L. 1976; Characterization of two endopolygalacturonase isoenzymes produced by Fusarium oxysporum f.splycopersici. Biochimica et biophysica acta 429:870–883
    [Google Scholar]
  14. Wang M. C., Keen N. T. 1970; Purification and characterization of endopolygalacturonase from Verticillium albo-atrum. Archives of Biochemistry and Biophysics 141:749–757
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-104-2-305
Loading
/content/journal/micro/10.1099/00221287-104-2-305
Loading

Data & Media loading...

Most cited this month Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error