Literature DB >> 2256947

Time profile of hemin aggregation: an analysis.

V Srinivas1, C M Rao.   

Abstract

The status of hemin, whether monomeric or aggregated, appears to be a key factor in deciding its biological activity. The molecular basis for the tendency of hemin to aggregate and the factors that regulate it are not yet fully understood. We have investigated the time profile of aggregation of hemin in aqueous solutions and the effect of temperature on the process of aggregation. Aggregation increases with increase in temperature. The time profile data, as monitored by change in absorbance at 398 nm, fits a nonlinear equation with three time constants, suggesting a possibility of three processes. Interestingly, the variation of these three time constants with temperature are different.

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Year:  1990        PMID: 2256947

Source DB:  PubMed          Journal:  Biochem Int        ISSN: 0158-5231


  3 in total

1.  Speciation and structure of ferriprotoporphyrin IX in aqueous solution: spectroscopic and diffusion measurements demonstrate dimerization, but not mu-oxo dimer formation.

Authors:  Katherine A de Villiers; Catherine H Kaschula; Timothy J Egan; Helder M Marques
Journal:  J Biol Inorg Chem       Date:  2006-09-14       Impact factor: 3.358

2.  Delineating distinct heme-scavenging and -binding functions of domains in MF6p/helminth defense molecule (HDM) proteins from parasitic flatworms.

Authors:  Victoria Martínez-Sernández; Mercedes Mezo; Marta González-Warleta; María J Perteguer; Teresa Gárate; Fernanda Romarís; Florencio M Ubeira
Journal:  J Biol Chem       Date:  2017-03-27       Impact factor: 5.157

3.  Apoglobin Stability Is the Major Factor Governing both Cell-free and in Vivo Expression of Holomyoglobin.

Authors:  Premila P Samuel; Lucian P Smith; George N Phillips; John S Olson
Journal:  J Biol Chem       Date:  2015-07-23       Impact factor: 5.157

  3 in total

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