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Investigation of wool protein heterogeneity using two‐dimensional electrophoresis with immobilised pH gradients
Author(s) -
Herbert Ben R.,
Chapman Anna L. P.,
Rankin Douglas A.
Publication year - 1996
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.1150170141
Subject(s) - isoelectric point , chemistry , electrophoresis , immobilized ph gradient , isoelectric focusing , chromatography , polyacrylamide gel electrophoresis , alkaline phosphatase , polyacrylamide , gel electrophoresis , biochemistry , enzyme , polymer chemistry
The heterogeneity of intermediate filament proteins (IFP) from wool has been investigated using two‐dimensional polyacrylamide gel electrophoresis with immobilised pH gradients in the first dimension. The charge heterogeneity has been confirmed with some of the IFP separated as a string of spots with similar molecular weight, but markedly different in isoelectric point (p I ). The molecular weight and p I distribution of the string of IFP changed after treatment with alkaline phosphatase, indicating that some of the heterogeneity is caused by phosphorylation.