tailieunhanh - Báo cáo khoa hoc : Isolation and characterization of type I antifreeze proteins from cunner,Tautogolabrus adspersus, order Perciformes

Antifreeze proteins (AFPs) are produced by many species of teleost fish that inhabit potentially lethal ice-laden seawater and afford them protec-tion from freezing. To date type I AFPs have been fully characterized in two teleost orders: Pleuronectiformes and Scorpaeniformes. | IFEBS Journal Isolation and characterization of type I antifreeze proteins from cunner Tautogolabrus adspersus order Perciformes Rod S. Hobbs1 Margaret A. Shears1 Laurie A. Graham2 Peter L. Davies2 and Garth. L. Fletcher1 1 Ocean Sciences Centre Memorial university of Newfoundland Canada 2 Department of Biochemistry Queen s University Kingston Canada Keywords amino acid sequence cDNA sequence convergent evolution seasonalcycle thermalhysteresis Correspondence G. L. Fletcher Ocean Sciences Centre MemorialUniversity of Newfoundland St John s NLA1C 5S7 Canada Fax 1 709 864 3220 Tel 1 709 864 3276 E-mail fletcher@ or garthfletcher@ Website http osc Home Received 17 May 2011 revised 15 July 2011 accepted 29 July 2011 doi Antifreeze proteins AFPs are produced by many species of teleost fish that inhabit potentially lethal ice-laden seawater and afford them protection from freezing. To date type I AFPs have been fully characterized in two teleost orders Pleuronectiformes and Scorpaeniformes. In this study we report the isolation and complete characterization of a type I AFP present in fish from a third order cunner Tautogolabrus adspersus order Perciformes family Labridae . This protein was purified from blood plasma and found to belong to what is now known as classical type I AFP with their small size mass Da alanine richness 57 mol high a-helicity 99 with the ability to undergo reversible thermal denaturation 11 amino acid ThrX10 repeat regions within the primary structure the capacity to impart a hexagonal bipyramidal shaping to ice crystals and the conservation of an ice-binding site found in many of the other type I AFPs. Partial de novo sequencing of the plasma AFP accounted for approximately half of the peptide mass. Sequencing of a combined liver and skin cDNA library indicated that the protein is produced without a signal sequence. In addition the translated product of the AFP cDNA suggests .

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