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Stability of a potential blood substitute, HbXL99 alpha, under high pressure.

Abstract：

:One important criteria for a plasma circulating hemoglobin blood substitute is resistance to subunit dissociation. For this reason, cross-linked hemoglobins (with low oxygen affinities) are being specifically designed to serve as potential blood substitutes. An example is HbXL99 alpha, cross-linked between the alpha-subunits [PNAS (1987) 84:7280]. In the study presented here, the effects of up to 2 kilobars of pressure on the intrinsic fluorescence of HbXL99 alpha, HbA, and myoglobin were compared. Hemoglobin solutions were studied between 0.01-0.1g% in potassium phosphate or Hepes buffers, pH 7.4. Results show HbA exhibits a decrease in fluorescence intensity as a function of pressure. In contrast, HbXL99 alpha as well myoglobin (a monomer) show essentially no significant intrinsic fluorescence changes as a function of pressure. These results suggest that HbXL99 alpha is stable as a tetramer up to approximately 2 kilobars of pressure. In addition, high pressure intrinsic fluorescence studies provide a suitable technique for determining the subunit stability of hemoglobins.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Hirsch RE,Friedman JM,Harrington JR,Scarlata SF,Harrington JP

doi

10.1006/bbrc.1994.1639

subject

Has Abstract

pub_date

1994-05-16 00:00:00

pages

1635-40

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006291X84716391

journal_volume

200

pub_type

杂志文章

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