OJMS  Vol.1 No.2 , July 2011
Mechanisms of the Plurality of Scorpaena Porcus L. Serum Albumin
Author(s) A. M. Andreeva
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.

Cite this paper
A. Andreeva, "Mechanisms of the Plurality of Scorpaena Porcus L. Serum Albumin," Open Journal of Marine Science, Vol. 1 No. 2, 2011, pp. 31-35. doi: 10.4236/ojms.2011.12003.
References
[1]   E. A. Tinaeva, L. G. Markovich, V. V. Konkina and E. A. Semikrasova, “About Possibility of Blood Proteins Polymorphism Using as the Index of Selection in Fur Farming,” Vestnik, Vol. 11, No. 1, 2007, pp. 122-130.

[2]   F. A. Robey, T. Tanaka and T. Y. Liu, “Isolation and Characterization of Two Major Serum Proteins from the Dogfish, Mustelus Canis, C-Reactive Protein and Amyloid P Component,” The Journal of Biological Chemistry, Vol. 258, No. 6, 1983, pp. 3889-3894.

[3]   V. S. Kirpichnikov, “Genetika I Selektsija Ryb,” Nauka, Leningrad, 1987, p. 520.

[4]   L. Byrnes and F. Gannon, “Atlantic Salmon (Salmo Salar) Serum Albumin: cDNA Sequence, Evolution, and Tissue Expression,” DNA Cell Biology, Vol. 9, No. 9, 1990, pp. 647-565. doi:10.1089/dna.1990.9.647

[5]   P. J. Bentley, “A High-Affinity Zinc-Binding Plasma Protein in Channel Catfish (Ictalurus Punctatus),” Comparative Biochemistry and Physiology Part C: Comparative Pharmacology, Vol. 100, No. 3, 1991, pp. 491-494. doi:10.1016/0742-8413(91)90028-R

[6]   W. Nunomura, “C-Reactive Protein In Eel: Purification and Agglutinating Activity,” Biochimica et Biophysica Acta, Vol. 1076, No. 2, 1991, pp. 191-196. doi:10.1016/0167-4838(91)90265-2

[7]   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

[8]   V. Metcalf, S. Brennan, G. Chambers and P. George, “The Albumins of Chinook Salmon (Oncorhynchus tshawytscha) and Brown Trout (Salmo trutta) Appear to Lack a Propeptide,” Archives of Biochemistry and Biophysics, Vol. 350, No. 2, 1998, pp. 239-244. doi:10.1006/abbi.1997.0509

[9]   V. J. Metcalf, S. O. Brennan, G. K. Chambers and P. M. George, “The Albumin of the Brown Trout (Salmo trutta) is a Glycoprotein,” Biochimica et Biophysica Acta, Vol. 386, No. 1, 1998, pp. 90-96.

[10]   V. J. Metcalf, S. O. Brennan, G. K. Chambers and P. M. George, “High Density Lipoprotein (HDL), and Not Albumin, is the Major Palmitate Binding Protein in New Zealand Long-Finned (Anguilla dieffenbachii) and Short-Finned Eel (Anguilla australis schmidtii) Plasma,” Biochimica et Biophysica Acta, Vol. 1429, No. 2, 1999, pp. 467-475. doi:10.1016/S0167-4838(98)00260-X

[11]   V. J. Metcalf, S. O. Brennan and P. M. George, “The Antarctic Toothfish (Dissostichus mawsoni) Lacks Plasma Albumin and Utilises High Density Lipoprotein as Its Major Palmitate Binding Protein,” Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, Vol. 124, No. 2, 1999, pp. 147-155. doi:10.1016/S0305-0491(99)00051-6

[12]   V. Metcalf, S. Brennan and P. George, “Using Serum Albumin to Inter Vertebrate Phylogenies,” Applied Bioinformatics, Vol. 2, 2003, pp. 97-107.

[13]   V. J. Metcalf, P. M. George and S. O. Brennan, “Lungfish Albumin is More Similar to Tetrapod than to Teleost Albumins: Purification and Characterization of Albumin from Australian Lungfish, Neocaratodus Forsteri,” Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, Vol. 147, No. 3, 2007, pp. 428-437.

[14]   A. M. Andreeva, “Structural and Functional Organization of Albumin System of Fish Blood,” Journal of Ichthyology, Vol. 39, No. 9, 1999, pp. 788-794.

[15]   A. M. Andreeva, “Serum Peroxidases of Fish,” Journal of Ichthyology, Vol. 41, No. 1, pp. 104-111.

[16]   A. M. Andreeva, “The Structure of Serum Albumins of Fishes,” Zhurnal Evolyutsionnoi Biokhimii i Fiziologii, Vol. 46, No. 2, 2010, pp. 111-118.

[17]   A. M. Andreeva, “The Role of Structural Organization of Blood Plazma Proteins in the Stabilization of Water Metabolism in Bony Fish (Teleostei),” Journal of Ichthyology, Vol. 50, No. 7, 2010, pp. 552-558.

[18]   C. Szebedinszky and K. M. Gilmour, “The Buffering Power of Plasma in Brown Bullhead (Ameiurus nebulosus),” Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, Vol. 131, No. 2, 2002, pp. 171-183. doi:10.1016/S1096-4959(01)00492-4

[19]   Y. Xu and Z. Ding, “N-Terminal Sequence and Main Characteristics of Atlantic Salmon (Salmo salar) Albumin,” Preparative Biochemistry and Biotechnology, Vol. 35, No. 4, 2005, pp. 283-290. doi:10.1080/10826060500218081

[20]   A. M. Andreeva and R. A. Federov, “Features of the Organization of Low-Molecular Weight Proteins from the Blood and Tissue Fluid of the Common Stingray Dasyatis Pastinaca L. (Chondroichthyes: Trigonidae),” Russian Journal of Marine Biology, Vol. 36, No. 6, 2010, pp. 469-472.

[21]   L. L.Sulya, B. E. Box and G. Gordon, “Plasma Proteins in the Blood of Fishes from the Gulf of Mexico,” American Journal of Physiology, Vol. 200, No. 1, 1961, pp. 152-154.

[22]   H. De Smet, R. Blust and L. Moens, “Absence of Albumin in the Plasma of the Common Carp Cyprinus Carpio Binding of Fatty Acids to High Density Lipoprotein,” Fish Physiology and Biochemistry, Vol. 19, No. 1, 1998, pp. 71-81. doi:10.1023/A:1007734127146

[23]   A. M. Andreeva, I. P. Ryabtseva and V. V. Bolshakov, “Analysis of Permeability of Capillaries of Different Departments of Microcirculatory System for Plasma Proteins in Some Representatives of Bony Fishes,” Zhurnal Evolyutsionnoi Biokhimii i Fiziologii, Vol. 44, No. 2, 2008, pp. 212-214.

[24]   R. F. Itzhaki and D. M. Gill, “A Micro-Biuret Method for Estimating Protein,” Analytical Biochemistry, Vol. 9, No. 4, 1964, pp. 401-410. doi:10.1016/0003-2697(64)90200-3

[25]   U. K. Laemmli, “Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage,” Nature, Vol. 227, No. 5259, 1970, pp. 680-685.

[26]   A. E. Pinnel and B. E. Northam, “New Automated Dye-Binding Method for Serum Albumin Determination with Bromcresol Purple,” Clinical Chemistry, Vol. 24, No. 1, 1978, pp. 80-86.

[27]   A. M. Andreeva, “Identification of Serum Albumin and the Study Some of Its Physical Chemistry Properties in the Representatives of the Families Acipenseridae and Cyprinidae,” Inf Bull IBII AS USSR, Vol. 69, 1986, pp. 36-39.

[28]   A. M. Andreeva, “Physical Chemical Properties of Serum Albumin of the Blood from Acipenseridae and Cyprinidae on the Example to Sterljad and Bream. Physiology and the Biochemistry of the Hydrobionts,” Yaroslavl, 1987, pp. 108-114.

 
 
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