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Studies on 16 kDa selenium‐containing proteins enriched by means of preparative electrophoresis
Author(s) -
Kyriakopoulos Antonios,
Kalcklösch Margrit,
WeißNowak Christian,
Behne Dietrich
Publication year - 1993
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150140119
Subject(s) - chemistry , molecular mass , chromatography , selenium , differential centrifugation , gel electrophoresis , gel electrophoresis of proteins , sodium dodecyl sulfate , polyacrylamide gel electrophoresis , free flow electrophoresis , molecular weight size marker , fractionation , electrophoresis , centrifugation , two dimensional gel electrophoresis , biochemistry , proteomics , enzyme , organic chemistry , gene
Abstract By in vivo labeling with [ 75 Se]selenite and separation of the proteins in the tissue homogenates by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE), several selenium‐containing proteins or protein subunits were detected in rat tissues (liver, lung, spleen and prostate). Their distribution among the cell components was investigated after fractionation by means of differential centrifugation. The selenium‐containing proteins in the 16 kDa range were found to be mainly membrane‐bound. By two‐dimensional electrophoresis they were resolved into three labeled spots, two with the same relative molecular mass and p I values of about 4.8 and 5.0 and the third with a slightly lower molecular mass and a p I of 4.8. For further investigation they were concentrated and separeted from the other labeled compounds by SDS‐PAGE using preparative flow‐through electrophoresis.