Interaction of human fibrinogen with divalent metal chlorides

Maéda, Hiroshi; Kishi, Takaaki; Ikeda, Shôichi; Sasaki, Susumu; Kito, Kyoji

doi:10.1016/0141-8130(83)90031-4

Cited by 11 publications

(14 citation statements)

References 6 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…GST-(His) 6 was effectively precipitated using each of the metal ions tested. The effectiveness of the metal ions as precipitants followed the trend Zn 2+ > Cu 2+ > Ni 2+ , as was found in other work (Maeda et al, 1983), with this precipitation being reversed using EDTA.…”

Section: Frontal Analysis Of Gst-(his) 6 On Packed Beds Of Cu 2+ Nisupporting

confidence: 81%

“…Where the metal is leached by a protein possessing more than one highaffinity binding site, affinity precipitation can result. Metal affinity precipitation can occur with metal ions themselves (Maeda et al, 1983;Zaworski and Gill, 1988) in a similar way as has been used to separate proteins using metalloaded molecules such as ethylene glycol-bis(␤aminoethylether) N,N,NЈ,NЈ-tetraacetic acid (EGTA) (Carlsson et al, 1996;Larsson and Mosbach, 1979;Mejare et al, 1998). Experiments were therefore performed to investigate the batch precipitation of GST and GST-(His) 6 with various concentrations of Cu 2+ , Ni 2+ , and Zn 2+ and the dissolution of the precipitates with excess EDTA (data not shown).…”

Section: Frontal Analysis Of Gst-(his) 6 On Packed Beds Of Cu 2+ Nimentioning

confidence: 99%

See 1 more Smart Citation

Facilitated downstream processing of a histidine-tagged protein from unclarifiedE. coli homogenates using immobilized metal affinity expanded-bed adsorption

Clemmitt

Chase

2000

Biotechnol. Bioeng.

View full text Add to dashboard Cite

The facilitated downstream processing of an intracellular, polyhistidine‐tagged protein, glutathione S‐transferase [GST‐(His)6], direct from unclarified E. coli homogenates using expanded beds of STREAMLINE chelating, has been investigated. A series of pilot experiments were used to develop preparative‐scale separations of GST‐(His)6, initially in packed and then in expanded beds. Packed beds of Ni2+‐loaded STREAMLINE chelating proved to have the highest 5% dynamic capacity for GST‐(His)6, of 357 U mL−1 (36 mg mL−1). When using immobilized Cu2+ or Zn2+, metal ion transfer was observed from the iminodiacetate ligands to the high‐affinity chelator, GST‐(His)6. The subsequent metal affinity precipitation of this homodimer resulted in operational problems. An equilibrium adsorption isotherm demonstrated the high affinity of GST‐(His)6 for immobilized Ni2+, with a qm of 695 U mL−1 (70 mg mL−1) and a Kd of 0.089 U mL−1 (0.0089 mg mL−1). Ni2+‐loaded STREAMLINE chelating was therefore selected to purify GST‐(His)6 from unclarified E. coli homogenate, resulting in an eluted yield of 80% and a 3.34‐fold purification. The high dynamic capacity in the expanded mode of 357 U mL−1 (36 mg mL−1) demonstrates that this specific interaction was not affected by the presence of E. coli cell debris. © 2000 John Wiley & Sons, Inc. Biotechnol Bioeng 67: 206–216, 2000.

show abstract

Section: Frontal Analysis Of Gst-(his) 6 On Packed Beds Of Cu 2+ Nisupporting

confidence: 81%

Section: Frontal Analysis Of Gst-(his) 6 On Packed Beds Of Cu 2+ Nimentioning

confidence: 99%

Facilitated downstream processing of a histidine-tagged protein from unclarifiedE. coli homogenates using immobilized metal affinity expanded-bed adsorption

Clemmitt

Chase

2000

Biotechnol. Bioeng.

View full text Add to dashboard Cite

show abstract

“…13 Under in vitro conditions, divalent metal ions were also found to influence fibrinogen aggregation in aqueous solutions. 14,15 While Ca 2+ , Mg 2+ , and Mn 2+ ions were not effective up to 10 mM 15 or did not induce any aggregation at all, 14 Cu 2+ and Zn 2+ ions already caused fibrinogen aggregation at salt concentrations below 10 mM. 14 This aggregation behavior was also found to depend on fibrinogen concentration, ionic strength, and pH.…”

Section: Introductionmentioning

confidence: 96%

“…Under in vitro conditions, divalent metal ions were also found to influence fibrinogen aggregation in aqueous solutions. , While Ca 2+ , Mg 2+ , and Mn 2+ ions were not effective up to 10 mM or did not induce any aggregation at all, Cu 2+ and Zn 2+ ions already caused fibrinogen aggregation at salt concentrations below 10 mM . This aggregation behavior was also found to depend on fibrinogen concentration, ionic strength, and pH . The difference in critical aggregation concentration of fibrinogen in the presence of different divalent cations might be explained by salting out or salting in effects, which are closely related to the Hofmeister series .…”

Section: Introductionmentioning

confidence: 97%

Influence of Divalent Metal Ions on the Precipitation of the Plasma Protein Fibrinogen

et al. 2021

View full text Add to dashboard Cite

Fibrinogen nanofibers are very attractive biomaterials to mimic the native blood clot architecture. Previously, we reported the self-assembly of fibrinogen nanofibers in the presence of monovalent salts and have now studied how divalent salts influence fibrinogen precipitation. Although the secondary fibrinogen structure was significantly altered with divalent metal ions, morphological analysis revealed exclusively smooth fibrinogen precipitates. In situ monitoring of the surface roughness facilitated predicting the tendency of various salts to form fibrinogen fibers or smooth films. Analysis of the chemical composition revealed that divalent salts were removed from smooth fibrinogen films upon rinsing while monovalent Na + species were still present in fibrinogen fibers. Therefore, we assume that the decisive factor controlling the morphology of fibrinogen precipitates is direct ion−protein contact, which requires disruption of the ion-surrounding hydration shells. We conclude that in fibrinogen aggregates, this mechanism is effective only for monovalent ions, whereas divalent ions are limited to indirect fibrinogen adsorption.

show abstract

“…Also fibrinogen has been shown to form extensive aggregates and clots in the presence of some cations (Maeda et al, 1983; Steven et al, 1982) or oxygen‐containing multivalent acid anions like phosphate or citrate (Hämisch et al, 2019; Hense et al, 2021). Self‐association of fibrinogen has also been reported (Zuev et al, 2017).…”

Section: Introductionmentioning

confidence: 99%