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L. Vazquez-Moreno, J. Porath, S. F. Schluter and J. J. Marchalonis, “Purification of a Novel Heterodimer from Shark (Carcharhinus plumbeus) Serum by Gel-Immobilized Metal Chromatography,” Comparative Biochemistry and Physiology Part C: Comparative Pharmacology, Vol. 103, No. 3, 1992, pp. 563-568. doi:10.1016/0305-0491(92)90371-W

has been cited by the following article:

• TITLE: Mechanisms of the Plurality of Scorpaena Porcus L. Serum Albumin

  AUTHORS: A. M. Andreeva

  KEYWORDS: Scorpaena, Blood, Tissue Fluids, Low-Molecular Proteins, Albumin, Mass Spectrum, Duplications

  JOURNAL NAME: Open Journal of Marine Science, Vol.1 No.2, July 22, 2011

  ABSTRACT: The proteins, which bind albuminspecific dye Evans blue, are revealed in the low-molecular protein fraction of the blood serum from Scorpaena porcus L. and identified as serum albumin. They were represented by three bands in 2D-SDS-PAAG. MALDI-TOF-analysis revealed the fundamental similarity of the mass spec-trum of the fragments of tryptic cleavage of proteins with molecular weight 73 and 76 kDa. The role of du-plications and intragenic reconstructions in the creation of the plurality of scorpaena albumins is discussed.