PMID: 9181695Jun 15, 1997Paper

Characterization of a heat-stable fraction of lipovitellin and development of an immunoassay for vitellogenin and yolk protein in winter flounder (Pleuronectes americanus)

The Journal of Experimental Zoology
R C HartlingJ G Kunkel

Abstract

An enzyme-linked immunoabsorbent assay was developed for detection and quantification of the yolk protein lipovitellin (Lv) and its plasma precursor, vitellogenin (Vg), in winter flounder (Pleuronectes americanus). Native Lv was found to be a mixture of heat-stable and heat-labile molecules in mature, ovulated eggs. A heat-stable Lv fraction was purified from extracts of unfertilized eggs by brief heat treatment and gel permeation chromatography on Bio-Gel A-1.5. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) of heat-stable Lv revealed a single polypeptide of 94 kD, while native Lv also possessed several smaller polypeptides, suggesting that heat-labile Lv contains proteolytic cleavages of the 94-kD polypeptide which destabilize its structure. The Stokes radius of the native protein on Bio-Gel A-1.5 was estimated at 4.50 nm, while the Stokes radii of heat-stable and heat-labile Lv were 4.26 nm and 5.17 nm, respectively. Heat-stable Lv was used to produce a rabbit polyclonal antiserum which reacted with a single 175-kD polypeptide in Western blots of vitellogenic female winter flounder serum, but did not react with any component of male serum. Ouchterlony double diffusion using this antiserum demonstrated i...Continue Reading

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Citations

Mar 17, 2016·Comparative Biochemistry and Physiology. Toxicology & Pharmacology : CBP·Jun WangShaoguo Ru
Mar 18, 2008·General and Comparative Endocrinology·José M GuzmánEvaristo L Mañanós
Mar 8, 2012·Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology·Brande L JonesTerry W Snell
Sep 22, 2010·Marine Biotechnology·Jun Zhang, Shicui Zhang
Apr 2, 2021·General and Comparative Endocrinology·Rodolfo AmthauerLuis Vargas-Chacoff

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