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Related Experiment Videos

Peptidase activity in Tetrahymena.

M K Zdanowski, L Rasmussen

    Journal of Cellular Physiology
    |September 1, 1979
    PubMed
    Summary
    This summary is machine-generated.

    Peptidase activity in Tetrahymena thermophila occurs in the cytoplasm and on the cell surface. This study reveals how these protozoa utilize peptides for growth, independent of food vacuole formation.

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    Area of Science:

    • Biochemistry
    • Cell Biology
    • Microbiology

    Background:

    • Peptidases play crucial roles in cellular processes.
    • Understanding peptidase localization and specificity is vital for comprehending nutrient uptake in microorganisms.

    Purpose of the Study:

    • To investigate the localization of peptidase activity in Tetrahymena thermophila.
    • To characterize the specificity of cell-surface bound peptidases.
    • To determine in vivo peptidase specificities related to growth.

    Main Methods:

    • Incubation of Tetrahymena thermophila with peptides and measurement of extracellular amino acid concentrations.
    • Growth experiments using specific dipeptides as leucine donors.
    • Comparison of peptidase activity with and without food vacuole formation.

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    Main Results:

    • Peptidase activity was identified in both the cytoplasm and on the outer cell surface of Tetrahymena thermophila.
    • Surface-bound peptidases efficiently hydrolyze di- and tri-phenylalanine on a molar basis.
    • Tetrahymena thermophila and Tetrahymena pyriformis utilize L-leucyl-L-leucine but not L-leucyl-D-leucine as a leucine source for growth.

    Conclusions:

    • Tetrahymena thermophila possesses cytoplasmic and cell-surface peptidases.
    • Cell-surface peptidases contribute to peptide hydrolysis.
    • In vivo growth experiments demonstrate stereospecificity in leucine uptake via dipeptides.