Co++ binding by plasma proteins

Nandedkar, Arvind K.N.; Basu, Pankaj K.; Friedberg, Felix

doi:10.1016/s0006-3061(00)80158-1

Cited by 27 publications

(7 citation statements)

References 9 publications

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“…This could partially be related to a depletion of the Co content in the surface oxide, Figure 5; however, this cannot be a dominating effect. The authors suggest instead that Co strongly binds to albumin, as previously reported 5,[39][40][41] and that this may lead to protein aggregation 39 and hence precipitation of proteins from solution. This is also indicated by the significant underestimation (27%) of aqueous Co in PBS 1 BSA samples, based on measurements in solution by means of AAS, after given exposure periods and hence sufficient reaction time to form Co-protein complexes that aggregate and precipitate from solution (a nonsignificant effect when directly measured).…”

Section: Discussionmentioning

confidence: 69%

Metal release and speciation of released chromium from a biomedical CoCrMo alloy into simulated physiologically relevant solutions

Hedberg

Wallinder

2013

J Biomed Mater Res

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The objective of this study was to investigate the extent of released Co, Cr(III), Cr(VI), and Mo from a biomedical high-carbon CoCrMo alloy exposed in phosphate-buffered saline (PBS), without and with the addition of 10 µM H2 O2 (PBS + H2 O2 ), and 10 g L(-1) bovine serum albumin (PBS + BSA) for time periods up to 28 days. Comparative studies were made on AISI 316L for the longest time period. No Cr(VI) release was observed for any of the alloys in either PBS or PBS + H2 O2 at open-circuit potential (no applied potential). However, at applied potentials (0.7 V vs. Ag/AgCl), Cr was primarily released as Cr(VI). Co was preferentially released from the CoCrMo alloy at no applied potential. As a consequence, Cr was enriched in the utmost surface oxide reducing the extent of metal release over time. This passivation effect was accelerated in PBS + H2 O2 . As previously reported for 316L, BSA may also enhance metal release from CoCrMo. However, this was not possible to verify due to the precipitation of metal-protein complexes with reduced metal concentrations in solution as a consequence. This was particularly important for Co-BSA complexes after sufficient time and resulted in an underestimation of metals in solution.

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Section: Discussionmentioning

confidence: 69%

Metal release and speciation of released chromium from a biomedical CoCrMo alloy into simulated physiologically relevant solutions

Hedberg

Wallinder

2013

J Biomed Mater Res

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“…Although inorganic (non-B 12 -) cobalt is invariably present in organs and body fluids, its physiological role, if any, is unknown. Cobalt(II) ions are bound preferentially by serum albumin, which presumably also functions as the transport protein (Nandetkar et al 1972). …”

Section: 25mentioning

confidence: 99%

Cobalt

Schrauzer

2004

Elements and Their Compounds in the Environment

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“…The disappearance curve of 54Mn(II) is essentially parallel on a semi-log scale in the two groups though the administration of NTA markedly reduced the 54Mn(II) plasma concentration at every time interval, This suggests that injected 54Mn(II) results in the partition between two major components (a) the fast excretable 54Mn(II) plasma complex and (b) slow excretable non-chelated 54Mn(II) (Nandedkar et al 1973). Additionally, the 54Mn(II) NTA complex formed in experimental animals possibly competes with the 54Mn(II) plasma complex and resulting into the rapid excretion of the metal.…”

Section: Discussionmentioning

confidence: 87%