Hydrodynamic and Thermodynamic Properties of Bovine Serum Albumin at Low pH

Loeb, George I.; Scheraga, Harold A.

doi:10.1021/j150546a009

Cited by 111 publications

(23 citation statements)

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“…For ample and comprehensive study see Monkos [21]. The F form would have an 11% volume increase due to hydrodynamic radium change and its dimensions would be 40Å × 129Å [22]. The E form would undertake a new expansion resulting in 21Å × 250Å approximate dimensions [6].…”

Section: Resultsmentioning

confidence: 99%

Intrinsic viscosity of bovine serum albumin conformers

Curvale

Masuelli

Padilla

2008

International Journal of Biological Macromolecules

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Section: Resultsmentioning

confidence: 99%

Intrinsic viscosity of bovine serum albumin conformers

Curvale

Masuelli

Padilla

2008

International Journal of Biological Macromolecules

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“…1 shows that both BSA and alginate have no increase in acidity above pH 8.0, implying the predominance of carboxylic functional groups. Other researchers have also reported the presence of carboxylic functional groups in alginate [20,21] and BSA [21][22][23]. The profiles of BSA and alginate indicate that alginate has more carboxylic groups than BSA as the alginate acidity stabilizes at 3-3.5 meq/g, whereas the BSA acidity stabilizes at 1-1.5 meq/g.…”

Section: Potentiometric Titration Of Organic Foulantsmentioning

confidence: 87%

Protein (BSA) fouling of reverse osmosis membranes: Implications for wastewater reclamation

Ang

Elimelech

2007

Journal of Membrane Science

335

246

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“…DNA polymerase assays were performed at 370 essentially as described by Chang et al (7). For polymerase-a assays 25 Ml of solution to be assayed was combined with 100 ,l of an assay solution to give final concentrations of 40 mM potassium phosphate, pH 7.5, 10 mM 2-mercaptoethanol, 6 spotted on glass fiber filters and analyzed for acid-precipitable radioactivity. It should be noted that phosphate in the polymerase-f assays causes considerable inhibition, as noted by others (22); thus, the polymerase-fl activities reported represent about 25% of activities assayed in the absence of phosphate.…”

Section: Methodsmentioning

confidence: 99%

Intracellular localization of mouse DNA polymerase-alpha.

Herrick¹,

Spear²,

Veomett³

1976

Proc. Natl. Acad. Sci. U.S.A.

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Although DNA polymerase-a (DNA nucleotidyltransferase; deoxynucleoside triphosphate:DNA deoxynucleotidyltransferase; EC 2.7.7.7) probably functions in the nucleus, it is usually found predominantly in the nonnuclear fraction of disrupted cells. We have reexamined the intracellular location of this enzyme using cytochalasin-B-induced enucleation, a technique which avoids exposure of nuclei to extra-cellular conditions during cell fractionation. In conditions where viability of separated cell parts is high and recovery is quantitative, we find greater than 85% of total DNA polymerase-a (and DNA polymerase-P) activity in the nucleated cell fragments (karyoplasts), from which we conclude that the location in vivo of DNA polymerase-a is either nuclear or perinuclear. On the other hand, thymidine kinase (ATP:thymidine 5'-phosphotransferase, EC 2.7. MATERIALS AND METHODS Mouse L929 cells were grown in Eagle's minimum essential medium with 10% fetal calf serum (Kansas City Biological) and were judged to be mycoplasma-free by the following tests: cytoplasmic thymidine incorporation (19), surface appearance in the scanning electron microscope (performed by J. Meek and M. Clark), and conversion of uridine to uracil by cell extracts (20). Enucleation was performed by centrifugation at 370 in medium containing 10 .g/ml of cytochalasin B (Aldrich Chemical), after a pre-spin to remove weakly attached cells, as described elsewhere (21). Cytoplasts or untreated whole cells were removed by trypsin treatment, collected by a brief centrifugation 5.min at 300 X g), and gently resuspended in phosphate-b ffered saline. The karyoplasts were gently resuspended in the enucleation flasks in phosphate-buffered saline. Concentrations of whole cells, karyoplasts, and cytoplasts in the suspensions were determined by drying drops of known weight on microscope slides; these preparations were subsequently fixed, Feulgen stained, methyl green counter-stained, and all particles from each drop were scored as whole cells, karyoplasts, or cytoplasts. After samples were removed from the suspensions for counting and determination of intactness (trypan blue exclusion), the whole cells and cell parts were collected by a final centrifugation. Examination of supernatants indicated complete recovery (>99%) in the three pellets.For

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Hydrodynamic and Thermodynamic Properties of Bovine Serum Albumin at Low pH

Cited by 111 publications

References 0 publications

Intrinsic viscosity of bovine serum albumin conformers

Intrinsic viscosity of bovine serum albumin conformers

Protein (BSA) fouling of reverse osmosis membranes: Implications for wastewater reclamation

Intracellular localization of mouse DNA polymerase-alpha.

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