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Modification of Acrylamide Electrophoresis for Microspectrophotometric Analysis of Fish Plasma Proteins
Author(s) -
Balsano J. S.,
Rasch E. M.
Publication year - 1975
Publication title -
transactions of the american fisheries society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.696
H-Index - 86
eISSN - 1548-8659
pISSN - 0002-8487
DOI - 10.1577/1548-8659(1975)104<150:moaefm>2.0.co;2
Subject(s) - chromatography , electrophoresis , coomassie brilliant blue , polyacrylamide gel electrophoresis , acrylamide , gel electrophoresis of proteins , distilled water , albumin , staining , polyacrylamide , gel electrophoresis , two dimensional gel electrophoresis , chemistry , biology , enzyme , microbiology and biotechnology , biochemistry , monomer , polymer , proteomics , organic chemistry , genetics , gene
A technique for discontinuous electrophoresis that permits rapid and direct comparisons of multiple samples in thin sheets of polyacrylamide gel is described. The resulting electropherograms are suitable for screening for enzyme polymorphisms and for densitometric scanning and/or direct photographing after gels are stained for total proteins. Each gel sheet (110 × 90 × 0.8 mm) can be used for simultaneous separation of 10‐15 different samples. Since total voltage and the running time required for successful resolution of fine protein bands are reduced in this system, minimal heating occurs within the gel matrix during electrophoresis. Up to 120 different blood samples (8 gel sheets) can be processed in about 8 hrs. Gels are stained overnight in Coomassie Brilliant Blue, rinsed several times and stored in 7% acetic acid. Particular gel sectors are then transferred to distilled water and mounted on glass microslides for photography or for densitometric evaluation with a Leitz microspectrophotometer. This technique has evolved during the past decade to become an effective and efficient method to identify characteristic diferences in the electrophoretic mobilities of plasma enzymes and albumin fractions from several populations of poeciliid fishes.