Comparative structural and functional studies of avian and mammalian hemoglobins

• Autorzy: Ajloo D. , Moosavi-Movahedi A.A. , Sadeghi M. , Gharibi H.
• Języki publikacji: EN

Abstrakty

EN

Thermal stabilities of chicken, grey lag goose (Anser anser), turkey as avian hemoglobins (Hbs); and human, bovine, sheep and horse as mammalian Hbs in hemolysate form were investigated and compared with oxygen affinities taken from literature. The thermal stability was obtained from thermal profiles using tempera­ture scanning spectrophotometry. The buffer conditions were 50 mM Tris, pH 7.2, and 1 mM EDTA. The average of the inverse temperature transitions, average hydrophobicity, total van der Waals volume, partial molal volume and hydration po­tential were calculated by computational methods. The hemolysed avian Hbs have a lower oxygen affinity, higher thermal stability and higher self association than the mammalian Hbs. These observations are based on amino-acid composition, influence of ionic effectors, and the presence of Hb D in several avian Hbs. The results indicate that the avian Hbs have a more tense (T) conformation than the mammalian Hbs.

Słowa kluczowe

EN

mammalian hemoglobin; horse; sheep; mammal; hemoglobin; bird; thermodynamic stability; hydrophobicity; computational method; man; Anser anser; turkey; avian hemoglobin; grey lag goose; chicken; respiratory system

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2002
• Tom: 49
• Numer: 2
• Opis fizyczny: p.459-470,fig.

Twórcy

autor

Ajloo D.

• University of Tehran, Tehran, Iran

autor

Moosavi-Movahedi A.A.

autor

Sadeghi M.

autor

Gharibi H.

Bibliografia

• Adachi K, Kim J, Travitz R, Harano T, Asakura T. (1987) Effect of amino acid at the beta6 position on surface hydrophobicity, stability, solubility, and the kinetics of polymerization of hemoglobin. J Biol Chem.; 262: 12920-5.
• Adachi K, Kim JY, Konitzer P, Asakura T, Saviola B, Surrey S. (1993) Effects of beta6 amino acid hydrophobicity on stability of hemoglobin tetramers. FEBSLett.; 315: 47-50.
• Andersen ME, Gibson QH. (1971) A kinetic analysis of the binding of oxygen and carbon monoxide to Lamprey hemoglobin Petromyzon marinus and Petromyzon fluviatilis. J Biol Chem.; 246: 4790-9.
• Argos P, Mohana JKR, Hargrave PA. (1982) Structural prediction of membrane-bound proteins. Eur J Biochem.; 128: 565-75.
• Bard H, Fouron JC, Groth AM, Soukini MA, Cornet A. (1976) The adaptation of the fetal red cells of newborn lambs to extrauterine life: the role of 2,3-diphosphoglycerate and adult hemoglobin. Pediatr Res.; 10: 823-5.
• Bartels H, Hiller G, Reinhardt W. (1966) Oxygen affinity of chicken blood before and after hatching. Respir Physiol.; 1: 345-456.
• Bigelow CC, Channon M. (1976) Handbook of Biochemistry and Molecular Biology, Proteins. Fasma GD. ed, vol 1, pp 209-243. CRC Press, Cleveland, OH.
• Brygier J, De Bruin SH, Hoof MK, Rollema HS. (1975) The interaction of organic phosphates with human and chicken hemoglobin. Eur J Biochem.; 60: 379-83.
• Bull HB, Breese K. (1973) Thermal stability of proteins. Arch Biochem Biophys.; 158: 681-6.
• Bureau M, Banerjee R. (1976) Structure — volume relationships in hemoglobin A densitometric and dilatometric study of the oxy deoxy transformation. Biochimie.; 58: 403-7.
• Chalikian TV, Totrov M, Abagyan R, Breslauer KJ. (1996) The hydration of globular proteins as derived from volume and compressibility measurement: cross correlating thermodynamics and structural data. J Mol Biol.; 260: 588-603.
• Cho KC, Choy CL. (1980) Thermal stability of hemoglobin and myoglobin; effect of spin state. Biochim Biophys Acta.; 622: 320-30.
• Chothia S, Wodak S, Janin J. (1976) Role of subunit interfaces in the allosteric mechanism of hemoglobin. Proc Natl Acad Sci US A.; 73: 3793-7.
• Christensen EH, Dill DB. (1965) Oxygen dissociation of bird blood. J Biol Chem.; 109: 443-8.
• Clerbaux T, Gustin P, Detry B, Cao ML, Frans A. (1993) Comparative study of the oxyhemoglobin dissociation curve of four mammals: man, dog, horse and cattle. Comp Biochem Physiol Comp Physiol.; 106: 687-94.
• Cobb JA, Manning D, Kolatkar PR, Cox DJ, Riggs AF. (1992) Deoxygenation-link association of a tetrameric component of chicken hemoglobin. J Biol Chem.; 267: 1183-9.
• Coletta M, Ascenzi P, Santucci R, Bertollini A, Amiconi G. (1993) Interaction of inositol hexakisphosphate with liganded ferrous human hemoglobin. Direct evidence for two functionally operative binding sites. Biochim Biophys Acta.; 1162: 309-14.
• Gekko K, Hasegawa Y. (1986) Compressibility-structure relationship of globular proteins. Biochemistry.; 25: 6563-71.
• Goldsack DE. (1970) Relation between the hydrophobicity index to the thermal stability of homologous proteins. Biopolymers.; 9: 247-52.
• Gustin P, Clerbaux T, Williams E, Lakeux P, Lomba F, Frans A. (1988) Oxygen transport properties of blood in two different bovine breeds. Comp Biochem Physiol A.; 89: 553-8.
• Harrington DJ, Adachi K, Royer WE. (1997) The high resolution crystal structure of deoxyhemoglobin S. J Mol Biol.; 272: 398-407.
• Irback A, Sanderlin E. (2000) On the hydrophobicity correlation in protein chains. Biophys J.; 79: 2252-8.
• Janin J, Miller S, Chothia C. (1988) Surface, subunit interfaces and interior of oligomeric proteins. J Mol Biol.; 204: 155-64.
• Janin J, Chothia C. (1990) The structure of protein-protein recognition sites. J Biol Chem.; 265: 16027-30.
• Jiang X, Kowalski J, Kelly JW. (2001) Increasing protein stability using a rational approach combining sequence homology and structural alignment: stabilizing the WW domain. Protein Science; 10: 1454-65.
• Koehl P, Levitt M. (1999) Structure-based conformational preference of amino acids. Proc Natl Acad Sci U S A.; 96: 12524-9.
• Kharakoze DP, Sarvazyan AP. (1993) Hydrational and intrinsic compressibilities of globular proteins. Biopolymers.; 33: 11-26.
• Knapp JE, Oliveira MA, Xie Q, Ernst SR, Riggs AF. (1999) The structural and functional analysis of the hemoglobin D component from chicken. J Biol Chem.; 274: 6411-20.
• Kumar S, Tsai CJ, Nussinov R. (2000) Factor enhancing protein thermostability. Protein Engineering.; 13: 179-91.
• Lenfant C, Kooyman GL, Elsner R, Drabek CM. (1969) Respiratory function of blood of adult and fetus. Am J Physiol.; 216: 1598-600.
• Messana I, Angeletti M, Castagnola M, Sanctis GD, Stasio ED, Giardina B, Puciarelli S, Coletta M. (1998) Thermodynamics of inositol hexakisphosphate interaction with human oxyhemoglobin. It is effective in improving oxygen release from tetrameric hemoglobins. J Biol Chem.; 273: 15329-34.
• Moss BA, Hamilton EA. (1974) Chicken definitive erythrocyte hemoglobin. Biochim Biophys Acta.; 371: 379-91.
• Mu X, Makowski L, Magdoff-Fairchild B. (1998) Analysis of stability of hemoglobin S double strands. Biophys J.; 74: 655-68.
• Naderi-manesh H, Sadeghi M, Arab S, Moosavi-Movahedi AA. (2001) Prediction of protein surface accessibility states using information theory. Proteins; 42: 452-9.
• Ooi T, Oobatake M, Nemety G, Scheraga H. (1987) Accessible surface areas as a measure of thermodynamic parameters of hydration of peptides. Proc Natl Acad Sci U S A.; 84: 3086-90.
• Perutz MF. (1983) Species adaption in a protein molecule. Mol Biol Evol.; 1: 1-28.
• Petruzzelli R, Aureli G, Lania A, Galtieri A, Desideri A, Giardina B. (1996) Diving behavior and haemoglobin function: the primary structure of the alpha- and beta-chains of the sea turtle ( Caretta caretta) and its functional implications. Biochem J.; 316: 959-65.
• Prakash V, Timasheff SN. (1985) Calculation of partial specific volumes of proteins in 8 M urea solution. Methods Enzymol.; 117: 53-60.
• Reddy LR, Reddy KS, Surrey S, Adachi K. (1996) Role of hydrophobic amino acids at beta and beta 88 in stabilizing F helix conformation of hemoglobin S. J Biol Chem.; 271: 24564-8.
• Rollema H, Bauer C. (1979) The interaction of inositol pentaphosphate with the hemoglobins of highland and lowland geese. J Biol Chem.; 254: 12038-43.
• Shrake A, Rupley JA. (1973) Environment and exposure to solvent of protein atoms, lysozyme and insulin. J Mol Biol.; 79: 351-71.
• Tuker VA. (1972) Metabolism during flight in the laughing gulls, Larus articilla. Am J Physiol.; 222: 237-45.
• Urry DW, Gowda DC, Parker TM, Luan C, Reid MC, Harris CM, Pattanaik A, Harris RD. (1992) Hydrophobicity scale for proteins based on inverse temperature transitions. Biopolymers.; 32: 1243-50.
• Wagschal K, Tripet B, Hodges RS. (1999) De novo design of a model peptide sequence to examine the effects of single amino acid substitutions in the hydrophobic core on both stability and oligomerization state of coiled-coils. J Mol Biol.; 285: 785-803.
• Williams RC, Tsay KY. (1973) A convenient chromatographic method for the preparation of human hemoglobin. Anal Biochem.; 54: 137-45.
• Yang T, Olsen KW. (1988) Effect of crosslinking on the thermal stability of hemoglobins II. The stabilization of met-, cyanomet-, and carbonmonoxyhemoglobins A and S with bis(3,5-dibromosalycil) fumarate. Arch Biochem Biophys.; 261: 283-90.
• Yohe ME, Sheffield KM, Mukerji I. (2000) Solubility of fluromethemoglobin S, effect of phosphate and temperature on polymerization. Biophys J.; 78: 3218-26.
• Zamyatnin AA. (1972) Protein volume in solution. Prog Biophys Mol Biol.; 24: 107-23.
• Zhang J, Hua Z, Tame JRH, Lu G, Zhang R, Gu X. (1996) The crystal structure of a high oxygen affinity species of hemoglobin (Bar-headed goose hemoglobin in the oxy form). J Mol Biol.; 255: 484-93.