Addendum

Rossi‐Fanelli, A.; Cavaliere, R.; Mondovı̀, Bruno; Moricca, G

doi:10.1007/978-3-642-81080-0_5

Cited by 9 publications

(9 citation statements)

References 1 publication

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“…(11.31) has been swamped by increasing salt concentration. As would be expected, there is a close inverse relation between a and b of Eq (10)…”

supporting

confidence: 75%

Binding of water and electrolytes to proteins. An equilibrium dialysis study

Bull¹,

Breese²

1976

Biopolymers

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The technique of equilibrium dialysis has been used to study water and salt binding to egg albumin, to human carbon monoxide hemoglobin, and to bovine serum albumin. The salts used were CsCl, KCl, NaCl, LiCl, Gu·HCl, NaBr, Cs2SO4, K2SO4, Na2SO4, Li2SO4, and Gu2SO4. The amount of water bound by proteins depends on the probe being used. Sulfates tend to bind to proteins and they also increase the water binding. At saturation, about 41 and 140 mol Gu·HCl bind to 1 mol egg albumin and to 1 mol carbon monoxide hemoglobin, respectively. Both proteins are dehydrated by Gu·HCl. The hydrodynamic hydration of egg albumin as determined by viscosity appers to increase as the relative viscosity of the medium increases.

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“…(11.31) has been swamped by increasing salt concentration. As would be expected, there is a close inverse relation between a and b of Eq (10)…”

supporting

confidence: 75%

Binding of water and electrolytes to proteins. An equilibrium dialysis study

Bull¹,

Breese²

1976

Biopolymers

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“…The lack of inhibitory effect of hemoglobin support the suggestion that globin binds deuteroporphyrin IX at vacant heme-binding sites [21]. ful discussions and to Mr Terje Bj@rndal for skillful technical assistance.…”

Section: At Ph 74 Deuteroporphyrinsupporting

confidence: 59%

Studies on the uptake of porphyrin by isolated rat liver mitochondria with particular emphasis on the effect of hemin

Koller

1979

FEBS Letters

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“…Cytochrome bd concentration was determined from the reduced minus 'air-oxidized' difference absorption spectra using De 628-607 of 10.8 mM À1 cm À1 for the E. coli enzyme [18], and De 628-605 of 12 mM À1 cm À1 for the A. vinelandii enzyme [32]. The concentration of human hemoglobin (Hb), purified according to [33], is expressed on the heme basis, using e 555 of 12.5 mM À1 cm À1 for the deoxygenated state.…”

Section: Methodsmentioning

confidence: 99%

Interaction of the bacterial terminal oxidase cytochrome bd with nitric oxide

et al. 2004

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Cytochrome bd is a prokaryotic terminal oxidase catalyzing O 2 reduction to H 2 O. The oxygen-reducing site has been proposed to contain two hemes, d and b 595 , the latter presumably replacing functionally Cu B of heme-copper oxidases. We show that NO, in competition with O 2 , rapidly and potently (K i ¼ 100%34 nM at $70 lM O 2 ) inhibits cytochrome bd isolated from Escherichia coli and Azotobacter vinelandii in turnover, inhibition being quickly and fully reverted upon NO depletion. Under anaerobic reducing conditions, neither of the two enzymes reveals NO reductase activity, which is proposed in heme-copper oxidases to be associated with Cu B .

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Addendum

Cited by 9 publications

References 1 publication

Binding of water and electrolytes to proteins. An equilibrium dialysis study

Binding of water and electrolytes to proteins. An equilibrium dialysis study

Studies on the uptake of porphyrin by isolated rat liver mitochondria with particular emphasis on the effect of hemin

Interaction of the bacterial terminal oxidase cytochrome bd with nitric oxide

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