dc.creatorSekino T.
dc.creatorFocesi Jr. A.
dc.creatorBonaventura C.
dc.creatorBonaventura J.
dc.date1978
dc.date2015-06-30T12:53:13Z
dc.date2015-11-26T14:34:47Z
dc.date2015-06-30T12:53:13Z
dc.date2015-11-26T14:34:47Z
dc.date.accessioned2018-03-28T21:38:13Z
dc.date.available2018-03-28T21:38:13Z
dc.identifier
dc.identifierComparative Biochemistry And Physiology -- Part A: Physiology. , v. 61, n. 2, p. 223 - 226, 1978.
dc.identifier3009629
dc.identifier10.1016/0300-9629(78)90101-9
dc.identifierhttp://www.scopus.com/inward/record.url?eid=2-s2.0-0018221740&partnerID=40&md5=4f0cae78907d77560f8a3301857da32e
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/97661
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/97661
dc.identifier2-s2.0-0018221740
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1248206
dc.description1. 1. The radular myoglobin of the Brazilian sea hare, Aplysia brasiliana, has been isolated and its ligand binding properties have been characterized. The myoglobin is similar to the myoglobin of Aplysia limacina (a Mediterranean species), and has a lower oxygen affinity than does myoglobin of the sperm whale, Physeter macrocephalus. 2. 2. Aplysia brasiliana myoglobin is a monomer and binds oxygen and other heme ligands non-cooperatively. There is no evidence of pH sensitivity in these processes. 3. 3. The kinetics of ligand binding and dissociation are simple processes. The lower oxygen affinity of Aplysia brasiliana myoglobin relative to sperm whale myoglobin is associated with a much higher rate of oxygen dissociation, with first order rate constants of 125 sec-1 and 10 sec-1 respectively. © 1978.
dc.description61
dc.description2
dc.description223
dc.description226
dc.descriptionAnderson, Brunori, Weber, Fluorescence studies of Aplysia and sperm whale apomyoglobins (1970) Biochemistry, 24, pp. 4723-4729
dc.descriptionAntonini, Brunori, (1971) Hemoglobin and Myoglobin in their Reactions with Ligands, , North Holland, Amsterdam
dc.descriptionBlundell, Brunori, Curti, Bolognesi, Coda, Fumagalli, Ungaretti, Crystallization and preliminary X-ray diffraction studies on met-myoglobin from Aplysia limacina (1975) J. molec. Biol., 97, pp. 665-666
dc.descriptionBonaventura, Sullivan, Bonaventura, Effects of pH and anions on functional properties of hemoglobin from Lemur fulvus fulvus (1974) J. blol. Chem., 249, pp. 3768-3775
dc.descriptionBrunori, Antonini, Fasella, Wyman, Fanelli, Reversible thermal denaturation of Aplysia myoglobin (1968) J. molec. Biol., 34, pp. 497-504
dc.descriptionBrunori, Ughetta, Rotilio, Antonini, Wyman, Redox equilibrium of sperm-whale myoglobin, Aplysia myoglobin, and Chironomus thummi hemoglobin (1971) Biochemistry, 10, pp. 1604-1609
dc.descriptionBrunori, Giacometti, Antonini, Wyman, Denaturation of Aplysia myoglobin. Equilibrium study (1972) J. molec. Biol., 63, pp. 139-152
dc.descriptionGiacometti, Da Ros, Antonini, Brunori, Equilibrium and kinetics of the reaction of Aplysia myoglobin with azide (1975) Biochemistry, 14, pp. 1584-1588
dc.descriptionGuiseppe, Calabrese, Giacometti, Brunori, An electron paramagnetic resonance study of Aplysia myoglobin (1971) Biochimica et Biophysica Acta (BBA) - Protein Structure, 236, pp. 234-237
dc.descriptionPerutz, Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8 Å resolution: (1) X-ray analysis (1968) Nature, Lond., 219, pp. 29-32
dc.descriptionRiggs, Wolbach, Sulphydryl groups and the structure of hemoglobin (1956) The Journal of General Physiology, 39, pp. 585-605
dc.descriptionRossi-Fanelli, Antonini, A new type of myoglobin isolated and crystallized from the muscles of Aplysiae (1957) Biochemia (URSS), 22, pp. 344-355
dc.descriptionRossi-Fanelli, Antonini, Povoledo, Further study on myoglobin II. Chemical and biochemical properties of a new type of myoglobin in molluscs, in Neuberger, A (1960) Symposium on Protein Structure, pp. 143-147. , Methuen, London
dc.descriptionSekino, Ogo, Montouchet, Focesi, Jr., Denaturation of Aplysia brasiliana myoglobin (1976) Tenth International Congress of Biochemistry, p. 169. , Abstract volume
dc.descriptionTakano, Structure of myoglobin refined at 2.0 Å resolution. I. Crystallographic refinement of metmyoglobin for sperm whale (1977) J. molec. Biol., 110, pp. 537-568
dc.descriptionTakano, Structure of myoglobin refined at 2.0 Å resolution. II. Structure of deoxymyoglobin from sperm whale (1977) J. molec. Biol., 110, pp. 569-584
dc.descriptionTentori, Vivaldi, Carta, Marinucci, Massa, Antonini, Brunori, Amino acid sequence of Aplysia limacina myoglobin (1973) Int. J. Peptide Protein Res., 5, pp. 187-200
dc.descriptionWittenberg, Brunori, Wittenberg, Wyman, Kinetics of the reactions of Aplysia myoglobin with oxygen and carbon monoxide (1965) Archs Biochem. Biophys., 111, pp. 576-579
dc.languageen
dc.publisher
dc.relationComparative Biochemistry and Physiology -- Part A: Physiology
dc.rightsfechado
dc.sourceScopus
dc.titleFunctional Properties Of Aplysia Brasiliana Myoglobin
dc.typeArtículos de revistas


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