Literature DB >> 139403

Uptake of calcium ions into microsomes isolated from Physarum polycephalum.

T Kato, Y Tonomura.   

Abstract

Membranous vesicles (microsomes) were isolated from plasmodia of the acellular slime mold, Physarum polycephalum. The microsomes were about 0.2 about 0.2 micronM in diameter, and about 10 nm thick. The main protein component of the vesicles had a molecular weight of 100,000 daltons. Calcium ions were taken up by the microsomes only in the presence of Mg2+- ATP. The maximum amount of Ca2+ ions accumulated in the microsomes was 0.24 micronmole/mg protein. The Ca2+ uptake was not accelerated by oxalate. The ATPase [EC 3.6.1.3] activity required Ca2+ ions for full activation. The concentration of Ca2+ ions required for half-maximum activation was about 1 micronM. The Km and Vm values were 53 micronM and 1.6 micronmole/(mg-min), respectively. About 0.2 mole of Ca2+ ions was taken up by the microsomes, coupled with the hydrolysis of 1 mole of ATP. THE ATPase activity and Ca2+ uptake of the microsomes were not inhibited by sodium azide. Furthermore, electron microscopic examination showed that mitochondrial contamination was slight. These results suggest that a vesicular calcium transport system, analogous to the sacroplasmic reticulum in skeletal muscle, is involved in regulation of the Ca2+ concentration in plasmodia of Physarum.

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Year:  1977        PMID: 139403     DOI: 10.1093/oxfordjournals.jbchem.a131437

Source DB:  PubMed          Journal:  J Biochem        ISSN: 0021-924X            Impact factor:   3.387


  4 in total

1.  ATP-dependent Ca uptake into plant membrane vesicles.

Authors:  J Gross; D Marmé
Journal:  Proc Natl Acad Sci U S A       Date:  1978-03       Impact factor: 11.205

2.  Effects of caffeine and D2O on persistence and de novo generation of intrinsic oscillatory contraction automaticity in Physarum.

Authors:  K G Götz von Olenhusen; K E Wohlfarth-Bottermann
Journal:  Cell Tissue Res       Date:  1979-04-12       Impact factor: 5.249

3.  Monoclonal antibodies to the Ca2+ + Mg2+-dependent ATPase of sarcoplasmic reticulum identify polymorphic forms of the enzyme and indicate the presence in the enzyme of a classical high-affinity Ca2+ binding site.

Authors:  E Zubrzycka-Gaarn; G MacDonald; L Phillips; A O Jorgensen; D H MacLennan
Journal:  J Bioenerg Biomembr       Date:  1984-12       Impact factor: 2.945

4.  Enrichment of fibrillar cytoplasmic actomyosin in protoplasmic strands of Physarum polycephalum for the production of cell-free models.

Authors:  N J Pies; K E Wohlfarth-Bottermann
Journal:  Cell Tissue Res       Date:  1985       Impact factor: 5.249

  4 in total

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