Hiroshi Matsubara, Keishiro Wada, Ryuichi Masaki (auth.),'s Iron and Copper Proteins PDF

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By Hiroshi Matsubara, Keishiro Wada, Ryuichi Masaki (auth.), Kerry T. Yasunodu, Howard F. Mower, Osamu Hayaishi (eds.)

ISBN-10: 1468432702

ISBN-13: 9781468432701

ISBN-10: 1468432729

ISBN-13: 9781468432725

An Fe- and Cu-Protein Symposium was once hung on December 15-18, 1975 on the East West Center-University of Hawaii and was once subsidized through the United States-Japan Cooperative technological know-how software below the auspices of the nationwide technological know-how origin and the Japan Society for the advertising of technology. It was once well-known by way of the organizers of the symposium that metalloproteins are vitally important within the box of overall healthiness technology and a subject matter useful of dialogue by means of specialists from the USA, Japan and Europe. The assembly was once limited to Fe- and Cu-proteins yet this is often nonetheless a really wide subject material and consequently, chosen subject matters of present curiosity during this box have been selected. This ebook includes the accrued papers from lots of the symposium contributors. the subject material coated during this publication is split into 4 elements. those are: 1) the iron-sulfur proteins (which aren't part of the mitochondrial electron shipping system); 2) the iron-sulfur proteins and heme proteins of the mitochondrial electron delivery approach; three) different heme and nonheme iron proteins; and five) chosen copper proteins. The organizers of the symposium desire to exhibit their gratitude to the contributors, the consultation chairmen, and Drs. I.C. Gunsalus and E. Frieden who assisted within the association of the symposium.

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E. CRAMER Amido & -Carboxyl /Carbons 8 Std Val, Asn, Asp, Glu, ~/ Gln ~& other I carbons ISO 100 SO Fig. SA. Natural abundance 13C NMR spectrum of oxidized ~. maxima ferredoxin. 7, 1 M NaC1, containing 75% DZO. Chemical shift scale is relative to 1-trimethylsi1ylpropane-3-sulfonate standard. ~ 300,000 scans. UO 100 so o Fig. SB. Natural abundance l3 C NMR spectrum of S. maxima ferredoxin reduced with dithionite. Concentrations and pH are same as oxidized form. ~ 375,000 scans. 2-Fe FERREDOXINS 33 or one or more shifted peaks from the (8) isoleucines and/or the (7) leucines.

H. & Yasunobu, K. T. 955. J. Bio1. , 244, 4 (1969), 10. Sugeno, K. & Hatsubara, H. 2979. 11. K. O. Biochem. Biophys. Res. , 6Lf, 1 (1975), 399. 12. , Haniu, H .. K. O. Unpublished Manuscript. 13. , Cammack, R. & Matsubara, H. Biochem. , 1L,5, 1 (1975), 121. 14. , Shin, M. & Matsubara, H. J. Biochem. (Japan), ~, 6 (1974), 1217. 15. H. 16. , Mukai, K. & Kimura, T. Biophys. Res. , g, 3 (1973), 869. 17. D. F. Proc. Nat. Acad. , 70, 8 (1973), 2429. 18. , Wada, K. & Okunuki, K. Biophys. Acta, 180 (1969), 196.

The supernatant (Sl) was saved. The sedimented pellets were suspended in the sucrose solution and the differential centrifugation (700 x g for 10 min and 9,000 x g for 30 min) was repeated. The supernatant (S2) was saved. Most of adrenal ferredoxin were extracted in the Sl and S2 fractions. Mitochondrial pellets thus obtained were used for ~solation of NADPH-adrena1 ferredoxin reductase and cytochrome P-450. The Sl and S2 fractions containing adrenal ferredoxin were absorbed on a large column (5 x 25 cm) of DEAE cellulose.

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Iron and Copper Proteins by Hiroshi Matsubara, Keishiro Wada, Ryuichi Masaki (auth.), Kerry T. Yasunodu, Howard F. Mower, Osamu Hayaishi (eds.)

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