Open AccessInter-protein bonding and other molecular interactions in hen egg white
Author(s) -
M. Vuckovic,
Marija B. Radojčić,
H Bratoljub Milosavljevic
Publication year - 2000
Publication title -
journal of the serbian chemical society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.227
H-Index - 45
eISSN - 1820-7421
pISSN - 0352-5139
DOI - 10.2298/jsc0003157v
Subject(s) - egg white , ovalbumin , chemistry , polyacrylamide gel electrophoresis , chromatography , dissolution , fraction (chemistry) , gel electrophoresis , denaturation (fissile materials) , viscosity , electrophoresis , agglomerate , chemical engineering , biochemistry , materials science , enzyme , nuclear chemistry , organic chemistry , biology , immune system , immunology , composite material , engineering
The analysis of the SDS-polyacrylamide gel electrophoresis (SDS-PAGE) data, combined with the comparison of viscosity data corresponding to the thin fraction of hen egg white and 2 mM purefied ovalbumin solution, showed that the thin fraction is a protein solution. Dissolution of the thick fraction of hen egg white in SD Sandurea solutions followed by SDS-PAGE, in the presence or absence of b-mercaptoethanol, revealed that it is a protein gel. It was also found that the gel structure consists of the three-dimensional ovomucine- ovomucoid network (matrix) held together by S.S bridges which captures the rest of the proteins (ovalbumin, conalbumin, etc). The captured proteins can also be interconnected by S.S bridges thus forming agglomerates or conglomerates, but they are predominantly held by weak electrostatic interactions, as demonstrated by the washing out and dissolving experiments. The matrix structure does not prevent denaturation of the captured proteins as indecated by the 50% decrease in turbidity following gel swelling by the addition of 1 part of an8Murea solution to 9 parts of the gel.