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The Global ETD Search service is a free service for researchers
to find electronic theses and dissertations. This service is
provided by the
Networked Digital Library of Theses and Dissertations.
Our metadata is collected from universities around the world. If you manage a university/consortium/country archive and want to be added, details can be found on the NDLTD website.
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Showing 1 to 7 of 7 (0.033 seconds)Spelling suggestions: "subject:"ascarididae"" "subject:"ascaridia""
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Growth and development of the fourth-stage larvae of Ascaris suum Goeze, 1782.O'Grady, Richard Terence. January 1981 (has links)
No description available.
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| 2 |
Membrane properties and synaptic interactions of motorneurons in the nematode AscarisDavis, Ralph Eugene. January 1984 (has links)
Thesis (Ph. D.)--University of Wisconsin--Madison, 1984. / Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaves 230-231).
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| 3 |
Growth and development of the fourth-stage larvae of Ascaris suum Goeze, 1782.O'Grady, Richard Terence. January 1981 (has links)
No description available.
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| 4 |
The effects of certain anthelmintics on the tissue phase larvae of Ascaridia galli (Schrank, 1788)Persaud, Bhagirath R. B. January 1953 (has links)
Call number: LD2668 .T4 1953 P45 / Master of Science
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| 5 |
Some studies on the viability and development of the ova of Ascaridia lineata (Schneider)Cauthen, George Edward January 1931 (has links)
No description available.
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| 6 |
Nematode culture with special reference to Ascaridia lineata (Schneider)Todd, Arlie January 1938 (has links)
Typescript, etc.
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| 7 |
Purification and Characterization of Glycogen Synthase from Ascaris SuumHannigan, Linda L. (Linda Lucile) 08 1900 (has links)
Glycogen synthase, the enzyme that catalyzes the rate-limiting reaction of glycogen syntheses has been purified and characterized from Ascaris suum muscle. Glycogen in the crude extract was digested to release the enzyme, eluted from a DE52 cellulose column and then applied to a Sepharose affinity column. The purified Ascaris enzyme was found to be homologous to the mammalian enzyme with regard to subunit and holoenzyme Mr^3 allosteric activation, substrate affinity and covalent modification. However, the association between Ascaris glycogen synthase and endogenous glycogen differed from that in mammalian systems.
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