CAERULOPLASMIN AS DEMONSTRATED BY STARCH GEL ELECTROPHORESIS

Caeruloplasmin as demonstrated by starch gel electrophoresis.

Starch gel electrophoresis has demonstrated that graded concentrations of sodium sulphate do not precipitate the serum globulins in any reasonable degree of purity. The use of this form of electrophoresis has shown that caeruloplasmin is associated with a globulin in the Fa(2) position.This technique can be employed as a screening test for patients suspected of suffering from hepatolenticular d...

Distribution of the serum proteins of Syrian hamster as revealed by Starch gel electrophoresis

Starch-gel electrophoresis of rat-serum proteins.

In 1955, Smithies (1) described a procedure for the separation of human serum proteins by horizontal zone electrophoresis in starch gels. The separation of zones was improved by a later modification to a vertical electrophoresis in which the sample was inserted in the gel, free from supporting medium (2). With these methods, it has been demonstrated that many more protein fractions can be separ...

Fractionation of Bence-Jones protein by starch gel electrophoresis.

The development by Smithies (1955a) of starch gel as a medium for the electrophoresis of protein material marked an important advance, as it combines separation by electrical mobility with a form of pore filtration. Smithies (1955b) has been able to obtain 12 or more protein fractions from human serum with his one-dimensional technique and equally remarkable separation has been obtained with an...

Properties of alkaline-phosphatase fractions separated by starch-gel electrophoresis.