Abstract:
:Homogenates of Trypanoplasma borelli were subjected to subcellular fractionation by sequential differential and isopycnic centrifugation in sucrose. Glycerol-3-phosphate dehydrogenase and the glycolytic enzymes, glucosephosphate isomerase and triosephosphate isomerase, as well as the peroxisomal marker enzyme catalase were mainly, or in part, associated with sedimentable particles that had a buoyant density in sucrose of 1.22 g cm-3. Moreover, triosephosphate isomerase exhibited latency, both in total homogenates and in the particulate fraction. Electron microscopy of thin sections of T. borelli revealed the presence of microbodies that gave a positive reaction for catalase. Pyruvate kinase behaved as a typical soluble enzyme. It was stimulated by micromolar concentrations of fructose 2,6-bisphosphate and this stimulation was counteracted by inorganic phosphate in the millimolar range. The enzymes involved in the synthesis and degradation of fructose 2,6-bisphosphate, 6-phosphofructo-2-kinase and fructose-2,6-bisphosphatase, were both present in T. borelli and behaved as soluble enzymes. We conclude that in T. borelli the glycolytic pathway is compartmentalized in a way similar to that found in another Kinetoplastid family, the Trypanosomatidae, where seven glycolytic enzymes and two enzymes of glycerol metabolism are associated with glycosomes. Apparently the presence of glycosomes is a characteristic of all Kinetoplastida.
journal_name
Mol Biochem Parasitoljournal_title
Molecular and biochemical parasitologyauthors
Opperdoes FR,Nohynkova E,Van Schaftingen E,Lambeir AM,Veenhuis M,Van Roy Jdoi
10.1016/0166-6851(88)90108-9subject
Has Abstractpub_date
1988-08-01 00:00:00pages
155-63issue
2eissn
0166-6851issn
1872-9428pii
0166-6851(88)90108-9journal_volume
30pub_type
杂志文章abstract::Proteases play central roles in cell invasion by Toxoplasma gondii and other apicomplexan parasites. Herein we report the cloning and characterization of a novel secretory putative metalloproteinase, Toxolysin 4 (TLN4). T. gondii tachyzoites store TLN4 in the micronemes and secrete it in response to elevated calcium, ...
journal_title:Molecular and biochemical parasitology
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journal_title:Molecular and biochemical parasitology
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pub_type: 杂志文章
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更新日期:1987-12-01 00:00:00
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journal_title:Molecular and biochemical parasitology
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journal_title:Molecular and biochemical parasitology
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journal_title:Molecular and biochemical parasitology
pub_type: 杂志文章
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更新日期:1991-03-01 00:00:00
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更新日期:1999-08-20 00:00:00
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journal_title:Molecular and biochemical parasitology
pub_type: 杂志文章
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更新日期:1994-05-01 00:00:00
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更新日期:2016-05-01 00:00:00
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journal_title:Molecular and biochemical parasitology
pub_type: 杂志文章
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更新日期:2018-03-01 00:00:00
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journal_title:Molecular and biochemical parasitology
pub_type: 杂志文章
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更新日期:2000-12-01 00:00:00
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journal_title:Molecular and biochemical parasitology
pub_type: 杂志文章
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更新日期:2009-11-01 00:00:00
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journal_title:Molecular and biochemical parasitology
pub_type: 杂志文章
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journal_title:Molecular and biochemical parasitology
pub_type: 杂志文章
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更新日期:2008-02-01 00:00:00
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pub_type: 杂志文章
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journal_title:Molecular and biochemical parasitology
pub_type: 杂志文章
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更新日期:1984-07-01 00:00:00
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journal_title:Molecular and biochemical parasitology
pub_type: 杂志文章
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更新日期:1997-04-01 00:00:00
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journal_title:Molecular and biochemical parasitology
pub_type: 杂志文章
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更新日期:2001-03-01 00:00:00
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journal_title:Molecular and biochemical parasitology
pub_type: 杂志文章
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更新日期:1997-12-01 00:00:00