Literature DB >> 1567821

Dynamic light scattering investigations of human erythrocyte spectrin.

D M Budzynski1, A S Benight, C C LaBrake, L W Fung.   

Abstract

Dynamic light scattering measurements were performed on spectrin from human erythrocytes in 25 mM Tris buffer at pH 7.6 with 100 mM NaCl and 5 mM EDTA. Measurements were made on spectrin solutions prepared as dimers and tetramers over the temperature range from 23 to 41 degrees C, as a function of the square of the scattering vector (K2) over the range of 0.7 x 10(10) cm-2 less than or equal to K1 less than or equal to 20 x 10(10) cm-2. Analysis of the autocorrelation functions collected for these solutions revealed the presence of two predominant motional components over the entire range of K2. Plots of the diffusion coefficients (D20) of these components, with viscosity and temperature corrected to water at 20 degrees C, as a function of K2 indicated three rather distinct regions, flat regions at low and high K2 joined by a sloping intermediate region. At small K2 (less than or equal to 4 x 10(10) cm-2) the D20 values were (7.3 +/- 2.0) x 10(-8) cm2/s for the slow component and (20.3 +/- 2.0) x 10(-8) cm2/s for the fast component. At large K2 (greater than or equal to 10 x 10(10) cm-2) the values increased to (13.0 +/- 2.0) x 10(-8) cm2/s for the slow component and (39.4 +/- 2.0) x 10(-8) cm2/s for the fast component. In the intermediate K2 region, D20 is a linear function of K2 and appears as a transition between the low and high K2 regions.(ABSTRACT TRUNCATED AT 250 WORDS)

Entities:  

Mesh:

Substances:

Year:  1992        PMID: 1567821     DOI: 10.1021/bi00129a014

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


  4 in total

1.  Erythrocyte spectrin maintains its segmental motions on oxidation: a spin-label EPR study.

Authors:  L W Fung; B O Kalaw; R M Hatfield; M N Dias
Journal:  Biophys J       Date:  1996-02       Impact factor: 4.033

2.  Stabilization of the spectrin-like domains of nesprin-1α by the evolutionarily conserved "adaptive" domain.

Authors:  Zhixia Zhong; Siwei A Chang; Agnieszka Kalinowski; Katherine L Wilson; Kris Noel Dahl
Journal:  Cell Mol Bioeng       Date:  2010-06-01       Impact factor: 2.321

3.  Binding of hemin, hematoporphyrin, and protoporphyrin with erythroid spectrin: fluorescence and molecular docking studies.

Authors:  Debashree Das; Malay Patra; Abhijit Chakrabarti
Journal:  Eur Biophys J       Date:  2015-03-04       Impact factor: 1.733

4.  Probing conformational stability and dynamics of erythroid and nonerythroid spectrin: effects of urea and guanidine hydrochloride.

Authors:  Malay Patra; Chaitali Mukhopadhyay; Abhijit Chakrabarti
Journal:  PLoS One       Date:  2015-01-24       Impact factor: 3.240

  4 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.