Physical, biochemical and functional characterization of haemoglobin from three strains of Artemia

Sugumar Vasudevan1, Natesan Munuswamy
1Department of Zoology, University of Madras, Guindy Campus, Chennai 600025, TamilNadu, India. [email protected]

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Ar, 1970, Isolation and properties of the haemoglobin of the clam shrimp Cyzicus hierosolymitanus, Comp. Biochem. Physiol. B, 33, 481, 10.1016/0010-406X(70)90365-8

Azem, 1992, Structure of extracellular haemoglobin from the brine shrimp, Artemia salina, Comp. Biochem. Physiol. B, 101, 185, 10.1016/0305-0491(92)90176-R

Bowen, 1966, The genetics of Artemia salina, VI: summary of mutations, Biol. Bull., 131, 240, 10.2307/1539753

Bowen, 1969, The haemoglobins of Artemia salina, I: determination of phenotype by genotype and environment, Comp. Biochem. Physiol. B, 31, 733, 10.1016/0010-406X(69)92073-8

Bowen, 1976, The haemoglobins of Artemia salina, II: characterization, Comp. Biochem. Physiol. B, 55, 99, 10.1016/0305-0491(76)90180-2

Bowen, 1977, The haemoglobins of Artemia salina, IV: a model for genetic control of haemoglobin I, haemoglobin II and haemoglobin X, Biochem. Genet., 15, 409, 10.1007/BF00520187

Bowen, 1978, Artemia haemoglobin: genetic variation in parthenogenetic and zygogenetic populations, Biol. Bull., 155, 273, 10.2307/1540952

De Voeght, 1981, Structural characterization by biophysical methods of extracellular haemoglobin from the nematode Ascaris suum, Comp. Biochem. Physiol. B, 99, 425

Fish, 1970, Gel chromatography of proteins in denaturing solvents. Comparison between sodium dodecyl sulfate and guanidine hydrochloride as denaturants, J. Biol. Chem., 245, 5166, 10.1016/S0021-9258(18)62832-7

Fox, 1948, The haemoglobin in Daphnia, Proc. R. Soc. Lond., 135B, 195, 10.1098/rspb.1948.0006

Gallardo, 1987, Reproduction and genetics of Mexican Artemia, 249

Gilchrist, 1954, Haemoglobin in Artemia, Proc. R. Soc. Lond., 143B, 136, 10.1098/rspb.1954.0059

Gratzer, 1961, Electrophoretic behaviour of haemoglobin in agar gel, J. Chromatogr., 5, 315, 10.1016/S0021-9673(01)92863-8

Guadagnoli, 2005, Environmental hypoxia influences haemoglobin subunit composition in the branchiopod crustacean Triops longicaudatus, J. Exp. Biol., 208, 3543, 10.1242/jeb.01794

Heip, 1980, Artemia extracellular haemoglobins: ontogeny, structure and in vivo radiolabelling, 427

Helland, 2000, Modulation of the free amino acid pool and protein content in populations of the brine shrimp Artemia sp, Mar. Biol., 137, 1005, 10.1007/s002270000409

Hoshi, 1969, Studies on the physiology and ecology of planktons, XXIII: properties and O2 affinity of the Daphnia haemoglobins induced by the low oxygen culture, Sci. Rep. Niigata Univ., Ser. D: Biol., 6D, 155

Hourdez, 2005, Molecular and functional adaptations in deep-sea haemoglobins, J. Inorg. Biochem., 99, 130, 10.1016/j.jinorgbio.2004.09.017

Hourdez, 2000, Haemoglobin from a deep-sea hydrothermal vent copepod, Biol. Bull., 199, 95, 10.2307/1542868

Hundahl, 2003, Effects of water activity on oxygen-binding in high-molecular weight, extracellular invertebrate hemoglobin and hemocyanin, Comp. Biochem. Physiol. B, 136, 83, 10.1016/S1096-4959(03)00176-3

Ilan, 1979, Structural diversity of arthropod extracellular haemoglobins, Comp. Biochem. Physiol. B, 63, 303, 10.1016/0305-0491(79)90253-0

Kato, 2001, Two domain haemoglobin gene of the water flea Moina macrocopa: duplication in the ancestral Cladocera, diversification, and loss of a bridge intron, Gene, 273, 41, 10.1016/S0378-1119(01)00569-8

Kimura, 1999, Heterogeneity and differential expression under hypoxia of two-domain haemoglobin chains in the water flea, Daphnia magna, J. Biol. Chem., 274, 10649, 10.1074/jbc.274.15.10649

Kobayashi, 1981, Influences of haemoglobin concentration and temperature on oxygen uptake of Daphnia magna under low oxygen concentration, Comp. Biochem. Physiol. A, 69, 679, 10.1016/0300-9629(81)90155-9

Kobayashi, 1982, Influence of body size on haemoglobin concentration and resistance to oxygen deficiency in Daphnia magna, Comp. Biochem. Physiol. A, 72, 599, 10.1016/0300-9629(82)90130-X

Krissansen, 1981, A novel protease may explain widely differing models for the structure of Artemia salina haemoglobins, Biochim. Biophys. Acta, 671, 104, 10.1016/0005-2795(81)90100-8

Krissansen, 1983, Physical and biochemical characterization of artemocyanin, an abundant glycoprotein complex with latent proteolytic activity from the brine shrimp, Artemia, Biochim. Biophys. Acta, 747, 151, 10.1016/0167-4838(83)90133-4

Krissansen, 1984, Identification of the blue–green chromatophore of an abundant biliprotein from haemolymph of Artemia, Comp. Biochem. Physiol. B, 77, 249, 10.1016/0305-0491(84)90252-9

Laemmli, 1970, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature, 227, 680, 10.1038/227680a0

Mann, 1972, Protein polypeptide chain molecular weights by gel chromatography in guanidinium chloride, Methods Enzymol., 26, 28, 10.1016/S0076-6879(72)26004-9

Manwell, 1978, Haemoglobin in the Australian anostracan Parartemia zietziana: evolutionary strategies of conformity vs. regulation, Comp. Biochem. Physiol. A, 59, 17, 10.1016/0300-9629(78)90303-1

Marrink, 1969, Molecular weight determination by chromatography on Sepharose 4B, FEBS Lett., 2, 242, 10.1016/0014-5793(69)80031-1

Moens, 1976, The structure of Artemia salina haemoglobins: a comparative characterization of four naupliar and adult haemoglobins, Eur. J. Biochem., 67, 397, 10.1111/j.1432-1033.1976.tb10704.x

Moens, 1977, Characterization of the extracellular haemoglobins of Artemia salina, Biochem. J., 165, 111, 10.1042/bj1650111

Moens, 1978, Evidence for a dimeric form of Artemia salina extracellular haemoglobins with high-molecular weight subunits, Eur. J. Biochem., 82, 65, 10.1111/j.1432-1033.1978.tb11997.x

Moens, 1990, Structural interpretation of the amino acid sequence of a second domain from the Artemia covalent polymer globin, J. Biol. Chem., 265, 14285, 10.1016/S0021-9258(18)77298-0

Rousselot, 2006, Native and subunit molecular mass and quarternary structure of the hemoglobin from the primitive branchiopod crustacean Triops cancriformis, FEBS J., 273, 4055, 10.1111/j.1742-4658.2006.05408.x

Seidl, 2005, Acclimation of the microcrustacean Daphnia magna to warm temperatures is dependent on haemoglobin expression, J. Therm. Biol., 30, 532, 10.1016/j.jtherbio.2005.06.004

Sick, 1969, Method for the continuous registration of O2-binding curves of haemoproteins by means of a diffusion chamber, Anal. Biochem., 32, 362, 10.1016/S0003-2697(69)80002-3

Smaridge, 1956, Distribution of iron in Daphnia in relation to haemoglobin synthesis and breakdown, Quart. J. Microscop. Soc., 97, 205

Sterling, 1977, The haemoglobins of Artemia salina, II: genetic variation in haemoglobin 1, haemoglobin 2 and haemoglobin 3, Biochem. Genet., 15, 423, 10.1007/BF00520188

Svedburg, 1933, The molecular weight of erythrocruorin, J. Am. Chem. Soc., 55, 2834, 10.1021/ja01334a033

Tasch, 1963

Vandenberg, 2002, Variant subunit specificity in the quaternary structure of Artemia haemoglobin, Mol. Biol. Evol., 19, 1288, 10.1093/oxfordjournals.molbev.a004189

Van Den Branden, 1978, Functional properties of the haemoglobins of Artemia salina L, Comp. Biochem. Physiol. A, 60, 185, 10.1016/0300-9629(78)90228-1

Waring, 1970, The haemoglobins of Artemia salina, II: isolation of three haemoglobins, Int. J. Biochem., 1, 537, 10.1016/0020-711X(70)90020-0

Weber, 2003, Haemoglobin function in deep-sea and hydrothermal-vent endemic fish: Symenchelis parasitica (Anguillidae) and Thermarces cerberus (Zoarcidae), J. Exp. Biol., 206, 2693, 10.1242/jeb.00475

Wolf, 1987, Study of the oxygen binding properties of Artemia haemoglobins, 221

Wood, 1975, Physicochemical properties of Planorbis corneus erythrocruorin, Biochem. J., 149, 437, 10.1042/bj1490437

Wood, 1981, Biophysical characterization of Artemia salina (L.) extracellular haemoglobins, Biochem. J., 193, 353, 10.1042/bj1930353

Zeis, 2003, The process of hypoxic induction of Daphnia magna hemoglobin: subunit composition and functional properties, Comp. Biochem. Physiol. B, 134, 243, 10.1016/S1096-4959(02)00253-1