1996
DOI: 10.1111/j.1525-1594.1996.tb04413.x
|View full text |Cite
|
Sign up to set email alerts
|

Biophysical Studies on the Correction of Uremic Human Serum Albumin Binding Defects by In Vitro Charcoal Adsorption Treatment

Abstract: Spectrofluorimetry, flow microcalorimetry, and differential scanning microcalorimetry (DSMC) were used to study the conformation, binding function, and ligand loading of uremic albumin obtained from the blood plasma of 2 end-stage renal disease (ESRD) patients before and after charcoal plasma treatment at different pH values (3.0-9.0). The spectrofluorimetric patterns of conformational N-F transition at low pH (4.2-3.5) are practically identical for both samples of uremic human serum albumin (HSA) and control … Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
2
1

Citation Types

0
5
0

Year Published

1998
1998
2020
2020

Publication Types

Select...
5

Relationship

0
5

Authors

Journals

citations
Cited by 5 publications
(5 citation statements)
references
References 20 publications
0
5
0
Order By: Relevance
“…In the case of AC1 administration (group 2) there was a tendency toward the appearance of the thermodenaturation maximum within 62-63 C, while in the case of AC2 administration (group 3) there were a distinct maximum at 62.4 C and a qualitative change in the shape of melting thermogram similar to that of intact animals (group 4). As a result of such type of serum "cleansing" under the influence of AC2 administered into gastro-intestinal tract, albumin molecules can gradually recover their native conformation [35].…”
Section: Resultsmentioning
confidence: 99%
“…In the case of AC1 administration (group 2) there was a tendency toward the appearance of the thermodenaturation maximum within 62-63 C, while in the case of AC2 administration (group 3) there were a distinct maximum at 62.4 C and a qualitative change in the shape of melting thermogram similar to that of intact animals (group 4). As a result of such type of serum "cleansing" under the influence of AC2 administered into gastro-intestinal tract, albumin molecules can gradually recover their native conformation [35].…”
Section: Resultsmentioning
confidence: 99%
“…2d). This is mirrored by a shift to the left of the thermograms with a simultaneous decrease of T 1 , T 2 and an increase in the ratio ΔH 1 /ΔH 2 which occurs after extraction of the bound ligands [4]. …”
Section: Resultsmentioning
confidence: 99%
“…Acidification to pH 3 and then extraction with activated charcoal [13]has been the most studied method [14, 15, 16, 17]and this can restore the binding to normal, at least in quantitative terms. The qualitative nature of albumin after such restoration of binding has, however, received little attention although recent investigations with microcalorimetry have revealed changes in albumin conformation [4]. The use of a pH as low as 3 for extraction is not a practical therapeutic proposition at present and furthermore, this pH leads to an irreversible change in the native protein pattern of blood [18].…”
Section: Introductionmentioning
confidence: 99%
See 1 more Smart Citation
“…Recent investigations do reveal changes in conformation, binding, function, and ligand loading of uremic albumin in patients with end-stage renal disease. After treatment with charcoal adsorption, the enthalpies and tryptophan fluorescence of uremic serum approached those of normal serum [32]. Other amino acids such as histidine, which is treated as an essential amino acid in renal failure, could also be implicated.…”
Section: Physiological and Clinical Implicationsmentioning
confidence: 99%