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Volumn 1431, Issue 2, 1999, Pages 492-499

Kinetic analysis on nitric oxide binding of recombinant Prolixin-S, a nitric oxide transport protein from the bloodsucking bug, Rhodnius prolixus

Author keywords

Hemoprotein; NO carrier; Rhodnius prolixus; Salivary glands; Stopped flow spectrophotometry

Indexed keywords

CARRIER PROTEIN; FLUPHENAZINE; HEMOPROTEIN; NITRIC OXIDE; RECOMBINANT PROTEIN;

EID: 0032946091     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(99)00082-5     Document Type: Article
Times cited : (15)

References (31)
  • 1
  • 2
    • 0028947447 scopus 로고
    • Purification, partial characterization, and cloning of nitric oxide-carrying heme proteins (nitrophorins) from salivary glands of the blood-sucking insect Rhodnius prolixus
    • Champagne D.E., Nussenzveig R.H., Ribeiro J.M.C. Purification, partial characterization, and cloning of nitric oxide-carrying heme proteins (nitrophorins) from salivary glands of the blood-sucking insect Rhodnius prolixus. J. Biol. Chem. 270:1995;8691-8695.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8691-8695
    • Champagne, D.E.1    Nussenzveig, R.H.2    Ribeiro, J.M.C.3
  • 3
    • 9244254265 scopus 로고    scopus 로고
    • Purification, characterization and cDNA cloning of a novel anticoagulant of the intrinsic pathway, (prolixin-s), from salivary glands of the blood sucking bug Rhodnius prolixus
    • Sun J., Ymaguchi M., Yuda M., Miura K., Takeya H., Hirai M., Matsuoka H., Ando K., Watanabe T., Suzuki K., Chinzei Y. Purification, characterization and cDNA cloning of a novel anticoagulant of the intrinsic pathway, (prolixin-s), from salivary glands of the blood sucking bug Rhodnius prolixus. Thromb. Haemost. 75:1996;573-577.
    • (1996) Thromb. Haemost. , vol.75 , pp. 573-577
    • Sun, J.1    Ymaguchi, M.2    Yuda, M.3    Miura, K.4    Takeya, H.5    Hirai, M.6    Matsuoka, H.7    Ando, K.8    Watanabe, T.9    Suzuki, K.10    Chinzei, Y.11
  • 4
    • 0030879304 scopus 로고    scopus 로고
    • Expression, reconstitution and characterization of prolixin-S as a vasodilator. A salivary gland nitric-oxide-binding hemoprotein of Rhodnius prolixus
    • Yuda M., Higuchi K., Sun J., Kureishi Y., Ito M., Chinzei Y. Expression, reconstitution and characterization of prolixin-S as a vasodilator. A salivary gland nitric-oxide-binding hemoprotein of Rhodnius prolixus. Eur. J. Biochem. 249:1997;337-342.
    • (1997) Eur. J. Biochem. , vol.249 , pp. 337-342
    • Yuda, M.1    Higuchi, K.2    Sun, J.3    Kureishi, Y.4    Ito, M.5    Chinzei, Y.6
  • 5
    • 0029044597 scopus 로고
    • Purification and characterization of prolixin S (nitrophorin 2), the salivary anticoagulant of the blood-sucking bug Rhodnius prolixus
    • Ribeiro J.M.C., Schneider M., Guimaraes J.A. Purification and characterization of prolixin S (nitrophorin 2), the salivary anticoagulant of the blood-sucking bug Rhodnius prolixus. Biochem. J. 308:1995;243-249.
    • (1995) Biochem. J. , vol.308 , pp. 243-249
    • Ribeiro, J.M.C.1    Schneider, M.2    Guimaraes, J.A.3
  • 6
    • 0028029463 scopus 로고
    • High affinity histamine-binding and antihistaminic activity of the salivary nitric oxide-carrying heme protein (nitrophorin) of Rhodnius prolixus
    • Ribeiro J.M.C., Ann Walker F. High affinity histamine-binding and antihistaminic activity of the salivary nitric oxide-carrying heme protein (nitrophorin) of Rhodnius prolixus. J. Exp. Med. 180:1994;2251-2257.
    • (1994) J. Exp. Med. , vol.180 , pp. 2251-2257
    • Ribeiro, J.M.C.1    Ann Walker, F.2
  • 7
  • 9
    • 0027975453 scopus 로고
    • Nitric oxide: A physiologic messenger molecule
    • Bredt D.S., Snyder S.H. Nitric oxide: A physiologic messenger molecule. Annu. Rev. Biochem. 63:1994;175-195.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 175-195
    • Bredt, D.S.1    Snyder, S.H.2
  • 10
    • 0028228808 scopus 로고
    • Soluble guanylate cyclase from bovine lung: Activation with nitric oxide and carbon monoxide and spectral characterization of the ferrous and ferric states
    • Stone J.R., Marletta M.A. Soluble guanylate cyclase from bovine lung: Activation with nitric oxide and carbon monoxide and spectral characterization of the ferrous and ferric states. Biochemistry. 33:1994;5636-5640.
    • (1994) Biochemistry , vol.33 , pp. 5636-5640
    • Stone, J.R.1    Marletta, M.A.2
  • 11
    • 5844284193 scopus 로고    scopus 로고
    • Spectral and kinetic studies on the activation of soluble guanylate cyclase by nitric oxide
    • Stone J.R., Marletta M.A. Spectral and kinetic studies on the activation of soluble guanylate cyclase by nitric oxide. Biochemistry. 35:1996;1093-1099.
    • (1996) Biochemistry , vol.35 , pp. 1093-1099
    • Stone, J.R.1    Marletta, M.A.2
  • 13
    • 0021093438 scopus 로고
    • Reaction of nitric oxide with heme proteins: Studies on metmyoglobin, opossum methemoglobin, and microperoxidase
    • Sharma V.S., Isaacson R.A., John M.E., Waterman M.R., Chevion M. Reaction of nitric oxide with heme proteins: Studies on metmyoglobin, opossum methemoglobin, and microperoxidase. Biochemistry. 22:1983;3897-3902.
    • (1983) Biochemistry , vol.22 , pp. 3897-3902
    • Sharma, V.S.1    Isaacson, R.A.2    John, M.E.3    Waterman, M.R.4    Chevion, M.5
  • 14
    • 0028048310 scopus 로고
    • Interaction between nitric oxide and prostaglandin H synthase
    • Tsai A., Wei C., Kulmacz R.J. Interaction between nitric oxide and prostaglandin H synthase. Arch. Biochem. Biophys. 313:1994;367-372.
    • (1994) Arch. Biochem. Biophys. , vol.313 , pp. 367-372
    • Tsai, A.1    Wei, C.2    Kulmacz, R.J.3
  • 15
    • 0017112413 scopus 로고
    • Cooperativity in the dissociation of nitric oxide from hemoglobin
    • Moore E.G., Gibson Q.H. Cooperativity in the dissociation of nitric oxide from hemoglobin. J. Biol. Chem. 251:1976;2788-2794.
    • (1976) J. Biol. Chem. , vol.251 , pp. 2788-2794
    • Moore, E.G.1    Gibson, Q.H.2
  • 16
    • 0018087302 scopus 로고
    • The dissociation of NO from nitrosylhemoglobin
    • Sharma V.S., Ranney H.M. The dissociation of NO from nitrosylhemoglobin. J. Biol. Chem. 253:1978;6467-6472.
    • (1978) J. Biol. Chem. , vol.253 , pp. 6467-6472
    • Sharma, V.S.1    Ranney, H.M.2
  • 17
    • 0030993345 scopus 로고    scopus 로고
    • Nitric oxide binding and crystallization of recombinant nitrophorin I, a nitric oxide transport protein from the blood-sucking bug Rhodnius prolixus
    • Andersen J.F., Champagne D.E., Weichsel A., Ribeiro J.M.C., Balfour C.A., Dress V., Montfort W.R. Nitric oxide binding and crystallization of recombinant nitrophorin I, a nitric oxide transport protein from the blood-sucking bug Rhodnius prolixus. Biochemistry. 36:1997;4423-4428.
    • (1997) Biochemistry , vol.36 , pp. 4423-4428
    • Andersen, J.F.1    Champagne, D.E.2    Weichsel, A.3    Ribeiro, J.M.C.4    Balfour, C.A.5    Dress, V.6    Montfort, W.R.7
  • 19
    • 0344121004 scopus 로고
    • Grafit Ver. 2.0, Erithaws Software, Staines, UK
    • R.J. Leatherbarrow, Grafit Ver. 2.0, Erithaws Software, Staines, UK, 1990, pp. 187-206.
    • (1990) , pp. 187-206
    • Leatherbarrow, R.J.1
  • 20
    • 33845550159 scopus 로고
    • Nitric oxide ferrohemes: Kinetics of formation and photodissociation quantum yields
    • Rose E.J., Hoffman B.M. Nitric oxide ferrohemes: Kinetics of formation and photodissociation quantum yields. J. Am. Chem. Soc. 105:1983;2866-2873.
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 2866-2873
    • Rose, E.J.1    Hoffman, B.M.2
  • 21
    • 0023274482 scopus 로고
    • Reaction of nitric oxide with heme proteins and model compounds of hemoglobin
    • Sharma V.S., Traylor T.G., Gardiner R., Mizukami H. Reaction of nitric oxide with heme proteins and model compounds of hemoglobin. Biochemistry. 26:1987;3837-3843.
    • (1987) Biochemistry , vol.26 , pp. 3837-3843
    • Sharma, V.S.1    Traylor, T.G.2    Gardiner, R.3    Mizukami, H.4
  • 22
    • 0000399717 scopus 로고
    • Photochemistry of nitric oxide adducts of water-soluble iron (III) porphyrin and ferrihemoproteins studied by nanosecond laser photolysis
    • Hoshino M., Ozawa K., Seki H., Ford P.C. Photochemistry of nitric oxide adducts of water-soluble iron (III) porphyrin and ferrihemoproteins studied by nanosecond laser photolysis. J. Am. Chem. Soc. 115:1993;9568-9575.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 9568-9575
    • Hoshino, M.1    Ozawa, K.2    Seki, H.3    Ford, P.C.4
  • 23
    • 0028219453 scopus 로고
    • How does NO activate hemeproteins?
    • Tsai A. How does NO activate hemeproteins? FEBS Lett. 341:1994;141-145.
    • (1994) FEBS Lett. , vol.341 , pp. 141-145
    • Tsai, A.1
  • 24
    • 0026737394 scopus 로고
    • Nitric oxide release from a single cell measured in situ by a porphyrinic-based microsensor
    • Malinski T., Taha Z. Nitric oxide release from a single cell measured in situ by a porphyrinic-based microsensor. Nature. 358:1992;676-678.
    • (1992) Nature , vol.358 , pp. 676-678
    • Malinski, T.1    Taha, Z.2
  • 25
    • 0020484754 scopus 로고
    • Kinetic analysis of the recombination of NO with ferrihemoproteins by the flash photolysis method
    • Kobayashi K., Tamura M., Hayashi K. Kinetic analysis of the recombination of NO with ferrihemoproteins by the flash photolysis method. Biochemistry. 21:1982;729-732.
    • (1982) Biochemistry , vol.21 , pp. 729-732
    • Kobayashi, K.1    Tamura, M.2    Hayashi, K.3
  • 26
    • 70449159499 scopus 로고
    • The kinetics and equilibria of the reactions of nitric oxide with sheep haemoglobin
    • Gibson Q.H., Roughton F.J.W. The kinetics and equilibria of the reactions of nitric oxide with sheep haemoglobin. J. Physiol. 136:1957;507-526.
    • (1957) J. Physiol. , vol.136 , pp. 507-526
    • Gibson, Q.H.1    Roughton, F.J.W.2
  • 29
    • 0029875840 scopus 로고    scopus 로고
    • S-Nitrosohaemoglobin: A dynamic activity of blood involved in vascular control
    • Jia L., Bonaventura C., Bonaventura J., Stamler J.S. S-Nitrosohaemoglobin: a dynamic activity of blood involved in vascular control. Nature. 380:1996;221-226.
    • (1996) Nature , vol.380 , pp. 221-226
    • Jia, L.1    Bonaventura, C.2    Bonaventura, J.3    Stamler, J.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.