Literature DB >> 6884505

Interaction of antimycin with cytochrome b-561. A study in secretory granules and in plasma membrane isolated from chromaffin cells of bovine adrenal medulla.

A N Malviya, A Rendon, D Aunis.   

Abstract

Cytochrome b-561 in chromaffin granules interacts with antimycin and its alpha-peak shifts 1 nm towards red. When chromaffin granules were treated with Triton X-100 antimycin no effect was observed. Cytochrome b-561 is located in the plasma membrane isolated from the chromaffin cells. The plasma membrane b-561 does not seem to interact with antimycin. A number of NADH or NADPH (acceptor) oxidoreductase activity has been observed in isolated plasma membrane providing clues to the origin of plasma membrane dehydrogenase. The possible role of cytochrome b-561 in secretory granules other than its accredited energy conserving electron transport property is projected.

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Year:  1983        PMID: 6884505     DOI: 10.1016/0014-5793(83)80956-9

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  2 in total

1.  Stereospecific inositol 1,4,5-[32P]trisphosphate binding to isolated rat liver nuclei: evidence for inositol trisphosphate receptor-mediated calcium release from the nucleus.

Authors:  A N Malviya; P Rogue; G Vincendon
Journal:  Proc Natl Acad Sci U S A       Date:  1990-12       Impact factor: 11.205

2.  Plasma membrane lipids of bovine adrenal chromaffin cells.

Authors:  A N Malviya; M M Gabellec; G Rebel
Journal:  Lipids       Date:  1986-06       Impact factor: 1.880

  2 in total

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