DEVELOPMENT OF TREHALASE AND INVERTASE ACTIVITY IN NEUROSPORA.

Item request has been placed! ×
Item request cannot be made. ×
loading   Processing Request
Read More Add to Saved list
  • Author(s): HILL EP; SUSSMAN AS
  • Source:
    Journal of bacteriology [J Bacteriol] 1964 Dec; Vol. 88, pp. 1556-66.
  • Publication Type:
    Journal Article
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: American Society for Microbiology Country of Publication: United States NLM ID: 2985120R Publication Model: Print Cited Medium: Print ISSN: 0021-9193 (Print) Linking ISSN: 00219193 NLM ISO Abbreviation: J Bacteriol Subsets: OLDMEDLINE
    • Publication Information:
      Original Publication: Washington, DC : American Society for Microbiology
    • Subject Terms:
      Cytoplasm* ; Glycoside Hydrolases* ; Metabolism* ; Neurospora* ; Research* ; Spores* ; Spores, Fungal* ; Sucrase* ; Trehalase* ; beta-Fructofuranosidase*; Kinetics
    • Abstract:
      Hill, E. P. (University of Michigan, Ann Arbor), and A. S. Sussman. Development of trehalase and invertase activity in Neurospora. J. Bacteriol. 88:1556-1566. 1964.-The levels of trehalase and invertase found during the development of Neurospora have been studied. Invertase activity is highest in the mycelium after growth has been completed, whereas the most trehalase activity is found in ungerminated conidia. Both enzymes show the least activity in the ascospore. Although the specific activity of trehalase varies no more than 3-fold during the spore stages, there is a 60-fold change in the mycelium. Similar but less pronounced variations in the specific activity of invertase in the mycelium occur. The lowest ratios of invertase to trehalase activity in the soluble fraction are found in conidia and ascospores, except in dormant ascospores where the ratio approaches that of older mycelium. Similar results are obtained for the enzymes in the wall fraction, except for dormant and newly activated ascospores. Moreover, the walls of young mycelium appear to have relatively more trehalase than is found at all other times. The activities of both enzymes vary about 20-fold in the wall fraction, but invertase activity fluctuates more widely than that of trehalase. Invertase activity always exceeds that of trehalase, and the cytoplasmic fraction contains more activity than that of the wall. These results are shown to contradict the hypothesis that trehalase and invertase activities are coordinately controlled. Finally, the role of trehalase in the activation of ascospores is considered in the light of these results.
    • References:
      Aust J Exp Biol Med Sci. 1953 Dec;31(6):583-9. (PMID: 13149560)
      Plant Physiol. 1959 Jul;34(4):466-72. (PMID: 16655255)
      Arch Biochem Biophys. 1962 Mar;96:468-74. (PMID: 14473052)
      J Biol Chem. 1952 Mar;195(1):19-23. (PMID: 14938350)
      Arch Biochem Biophys. 1963 Sep;102:389-96. (PMID: 14072517)
      Genetics. 1953 Jul;38(4):360-74. (PMID: 17247443)
      J Histochem Cytochem. 1964 Jun;12:448-50. (PMID: 14200762)
      J Bacteriol. 1948 Mar;55(3):327-30. (PMID: 16561462)
      J Cell Comp Physiol. 1961 Aug;58:11-6. (PMID: 13725544)
      J Biol Chem. 1951 Nov;193(1):265-75. (PMID: 14907713)
      Science. 1959 Nov 13;130(3385):1343. (PMID: 17753095)
    • Contributed Indexing:
      Keywords: EXPERIMENTAL LAB STUDY*; GLYCOSIDE HYDROLASES*; KINETICS*; METABOLISM*; NEUROSPORA*; SPORES*; SUCRASE*
    • Accession Number:
      EC 3.2.1.- (Glycoside Hydrolases)
      EC 3.2.1.26 (beta-Fructofuranosidase)
      EC 3.2.1.28 (Trehalase)
      EC 3.2.1.48 (Sucrase)
    • Publication Date:
      Date Created: 19641201 Date Completed: 19961201 Latest Revision: 20210526
    • Publication Date:
      20221213
    • Accession Number:
      PMC277452
    • Accession Number:
      10.1128/jb.88.6.1556-1566.1964
    • Accession Number:
      14240937