Phosphatases in Normal and Reorganizing Stentors

Weisz, Paul B.

doi:10.2307/1538099

Cited by 14 publications

(1 citation statement)

References 6 publications

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“…Acid phosphatases have been localized in protozoa by a number of investigators ( 1,2,10,15,19,27,29,31). Muller and his associates ( 18,19,20,21,22) have concentrated their attention on Paramecium and Tetrahymena, where they have localized acid phosphatase in food vacuoles at the light microscope level.…”

Section: Discussionmentioning

confidence: 99%

An Ultrastructural Study of Ingestion and Digestion in Tetrahymena pyriformis*

Elliott

Clemmons

1966

The Journal of Protozoology

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SYNOPSIS. When the structures involved in digestive events in T. pyriformis are examined at the electron microscope level, some information is added to that long known from light microscopy. The food trapping mechanism consists of the three membranelles, undulating membrane, oral ribs, and a “valve” apparently closing the opening to the cytopharynx. Both of the latter structures are supported by microtubules. Fibers extend internally from the cytopharynx and are closely associated with the food vacuole as it forms. Clear vacuoles resembling pinocytic vacuoles appear to arise from differentiated areas of the pellicle and plasma membrane. These vacuoles may fuse with primary lysosomes. Hydrolases are thus contributed to the pinocytic vacuoles which may then fuse with food vacuoles. When first formed food vacuoles contain no hydrolases but may acquire them directly, from primary lysosomes or from pinocytic vacuoles. Digestion proceeds to completion in the food vacuole, at which time soluble food products are released to the cytoplasm. Undigested materials are lost through the cytopyge. In stationary growth phase cells autophagic vacuoles form containing mitochondria and other cellular particulates. Such vacuoles probably contain hydrolases when formed and they may receive others by fusion with primary lysosomes.

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Section: Discussionmentioning

confidence: 99%

An Ultrastructural Study of Ingestion and Digestion in Tetrahymena pyriformis*

Elliott

Clemmons

1966

The Journal of Protozoology

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The nature of the phosphatases associated with nucleotide metabolism in Tetrahymena pyriformis

Conner

MacDonald

1964

J. Cell. Comp. Physiol.

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Observations on acid phosphatase in Mayorella palestinensis

Lasman

1967

Journal Cellular Physiology

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Acid phosphatzse activity has been studied in the ameba Mayorella palestinensis. Optimum activity of the enzyme was found to be at a pH of 3.2. The enzyme is inhibited by fluoride ion, but is not sensitive to Mg++.The activity was found to be correlated with age of culture. Two maxima have been obtained, one from cultures in the logarithmic phase, and the other during the period of maximal cell encystation. These results suggest that acid phosphatase play an important role in cell metabolism during growth and differentiation processes of this ameba.

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Phosphatases in Normal and Reorganizing Stentors

Cited by 14 publications

References 6 publications

An Ultrastructural Study of Ingestion and Digestion in Tetrahymena pyriformis*

An Ultrastructural Study of Ingestion and Digestion in Tetrahymena pyriformis*

The nature of the phosphatases associated with nucleotide metabolism in Tetrahymena pyriformis

Observations on acid phosphatase in Mayorella palestinensis

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