1990
DOI: 10.3109/10731199009117300
|View full text |Cite
|
Sign up to set email alerts
|

On the Hydrodynamic Instability of Hemoglobin Solutions

Abstract: The formation of heterogeneous fibers well observable under a magnifying glass in stirred "stroma-free" hemolysates of outdated banked erythrocytes was found to be predominantly due to random surface denaturation of both hemoglobin and non-heme proteins at the air-liquid interface. Electrophoretic analysis revealed that the precipitated and washed fibers contain residual membrane proteins as well as a certain amount of hemoglobin. The latter, however, largely remains in solution.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2

Citation Types

0
3
0

Year Published

1991
1991
2001
2001

Publication Types

Select...
4

Relationship

0
4

Authors

Journals

citations
Cited by 4 publications
(3 citation statements)
references
References 5 publications
0
3
0
Order By: Relevance
“…Sterilization is usually achieved by filtration or pasteurization in the carbonmonoxyHb form. Denaturation was also observed when Hb solutions were agitated while exposed to an air−liquid interface …”
Section: Hemoglobin Purificationmentioning
confidence: 99%
See 1 more Smart Citation
“…Sterilization is usually achieved by filtration or pasteurization in the carbonmonoxyHb form. Denaturation was also observed when Hb solutions were agitated while exposed to an air−liquid interface …”
Section: Hemoglobin Purificationmentioning
confidence: 99%
“…Denaturation was also observed when Hb solutions were agitated while exposed to an air-liquid interface. 563 Long-term storage of Hb is made difficult due to autoxidation. MetHb formation has been slowed by reducing temperature, controlling pH (metHb forms less rapidly above pH 7.0), increasing concentration, and addition of ascorbic acid and deferoxamine.…”
Section: Hemoglobin Purificationmentioning
confidence: 99%
“…The reductase system generates NADPH, an oxygen-linked cofactor (14), as a reaction product, and its concentration depends on the turnover of the reducing system, adding another variable to the reaction. In addition to being slow, gas-exchange experiments promote protein denaturation at the gas-liquid interface (15). In any case, when single-wavelength analysis is used, neither methemoglobin formation nor protein denaturation during the reaction can be quantified during the reaction process.…”
mentioning
confidence: 99%