Literature DB >> 999879

Studies on metrizamide-protein interactions.

A Hüttermann, G Wendlberger-Schieweg.   

Abstract

1. The apparent density of catalase after isopycnic centrifugation in metrizamide gradients is dependent on the metrizamide concentration into which the enzyme is dissolved at the beginning of the centrifugation. 2. This different behaviour of the enzyme in metrizamide gradients is due to the formation of a metrizamide-protein complex which is more dense than the uncomplexed catalase. 3. A bimodal distribution of the catalase, with additional heavy bands, was only observed in metrizamide gradients in light water, where rather high metrizamide concentrations are needed even for a banding of the uncomplexed enzyme. 4. The half-life of the metrizamide-protein complex is less than 5 min. This was shown by spectroscopical measurements and band sedimentation analysis in an analytical ultracentrifuge.

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Year:  1976        PMID: 999879     DOI: 10.1016/0005-2795(76)90261-0

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  4 in total

1.  Further characterization of the replicative complex of vesicular stomatitis virus.

Authors:  C C Simonsen; V M Hill; D F Summers
Journal:  J Virol       Date:  1979-08       Impact factor: 5.103

2.  Light-mediated Activation of Nitrate Reductase in Synchronous Chlorella.

Authors:  R Tischner
Journal:  Plant Physiol       Date:  1978-08       Impact factor: 8.340

3.  Isolation of the non-glycosylated proteins of desmosomes and immunolocalization of a third plaque protein: desmoplakin III.

Authors:  G Gorbsky; S M Cohen; H Shida; G J Giudice; M S Steinberg
Journal:  Proc Natl Acad Sci U S A       Date:  1985-02       Impact factor: 11.205

4.  Isolation of the intercellular glycoproteins of desmosomes.

Authors:  G Gorbsky; M S Steinberg
Journal:  J Cell Biol       Date:  1981-07       Impact factor: 10.539

  4 in total

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