scholarly journals Transformation of the water soluble fraction from “alpeorujo” by Coriolopsis rigida: The role of laccase in the process and its impact on Azospirillum brasiliense survival

Chemosphere ◽  
2010 ◽  
Vol 78 (1) ◽  
pp. 72-76 ◽  
Author(s):  
Mario C.N. Saparrat ◽  
Miguel Jurado ◽  
Rosario Díaz ◽  
Inmaculada Garcia Romera ◽  
María Jesús Martínez
2014 ◽  
Vol 91 (5) ◽  
pp. 473-481 ◽  
Author(s):  
Guiai Jiao ◽  
Xiangjin Wei ◽  
Gaoneng Shao ◽  
Lihong Xie ◽  
Zhonghua Sheng ◽  
...  

1957 ◽  
Vol 35 (4) ◽  
pp. 241-250 ◽  
Author(s):  
W. G. Martin ◽  
J. E. Vandegaer ◽  
W. H. Cook

Livetin, the major water-soluble protein of hen egg yolk, was found to contain three major components having mobilities of −6.3, −3.8, and −2.1 cm.2 sec.−1 volt−1 at pH 8, µ 0.1, and these have been designated α-, β-, and γ-livetin respectively. The α- and β-livetins were separated and purified electrophoretically after removal of γ-livetin by precipitation from 37% saturated ammonium sulphate or 20% isopropanol. The α-, β-, and mixed livetins resembled pseudoglobulins in solubility but γ-livetin was unstable and this loss of solubility has, so far, prevented its characterization. Molecular weights determined by light scattering, osmotic pressure, and Archibald sedimentation procedure yielded respectively: 8.7, 7.8, and 6.7 × 104 for α-livetin, and 4.8, 5.0, and4.5 × 104 for β-livetin. Under suitable conditions of sedimentation and electrophoresis, egg yolk has been shown to contain three components having the same behavior as the three livetins of the water-soluble fraction.


Chemosphere ◽  
2010 ◽  
Vol 78 (11) ◽  
pp. 1301-1312 ◽  
Author(s):  
S.M. Rodrigues ◽  
B. Henriques ◽  
J. Coimbra ◽  
E. Ferreira da Silva ◽  
M.E. Pereira ◽  
...  

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