Preparation and the hæmoglobin content of red cell ‘ghosts’
Preparation and the hæmoglobin content of red cell ‘ghosts’"
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ABSTRACT STUDIES of species differences in red cell phosphatides1 have led to a re-examination of the problem of standardizing the method of preparing erythrocyte membranes (‘ghosts’,
post-hæmolytic residues). It seems essential that if results obtained with physical methods, for example, electron microscopy, are to be correlated with those obtained by chemical analysis,
greater uniformity of procedure for preparation of membranes must be sought. The matter has received little recent attention. In what was perhaps the first chemical analysis of the
structural protein, stromatin, Jorpes2 found his preparations to contain irregular amounts of hæmoglobin, representing 10–30 per cent of the dry weight. Not long afterwards, Adams3 offered
spectroscopic evidence for the idea that in the intact cell hæmoglobin is combined with stromatin. Keilin and Hartree4, however, were able to show that the finding was explained by the
peculiar optical properties of the medium and could not be regarded as an indication of a hæmoglobin–stromatin complex. Since that time the blood-pigment found attached to ‘ghosts’ has come
to be regarded, or, at any rate, treated, as a sort of contaminant the physical association of which with the membrane proper interferes with obtaining satisfactory material for analysis of
other things. Various methods have been devised for preparing ‘ghosts’, one of which5 claims to reduce the iron content to the vanishing point (<0.01 per cent hæmoglobin). It is difficult
to find information about the stage in the processing at which the intact membranes begin to break up, or, indeed, what the microscopic appearance of the final product is. Usually, the
recommended techniques introduce acid or salt washing at some point to expedite the removal of hæmoglobin—measures which in our hands have led to prompt disintegration of ‘ghosts’, as shown
by microscopic examination. Access through your institution Buy or subscribe This is a preview of subscription content, access via your institution ACCESS OPTIONS Access through your
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FAQs * Contact customer support SIMILAR CONTENT BEING VIEWED BY OTHERS CYTOPLASMIC ANION/CATION IMBALANCES APPLIED ACROSS THE MEMBRANE CAPACITANCE MAY FORM A SIGNIFICANT COMPONENT OF THE
RESTING MEMBRANE POTENTIAL OF RED BLOOD CELLS Article Open access 02 September 2022 QUANTITATIVE ANALYSIS OF RED BLOOD CELL MEMBRANE PHOSPHOLIPIDS AND MODULATION OF CELL-MACROPHAGE
INTERACTIONS USING CYCLODEXTRINS Article Open access 15 September 2020 FERRITIN MICROHETEROGENEITY, SUBUNIT COMPOSITION, FUNCTIONAL, AND PHYSIOLOGICAL IMPLICATIONS Article Open access 14
November 2023 REFERENCES * Turner, J. C., Anderson, Helen M., and Gandal, C. P., _Biochim. Biophys. Acta_, 30, 130 (1958). Article CAS Google Scholar * Jorpes, E., _Biochem. J._, 26, 1488
(1932). Article CAS Google Scholar * Adams, G. A., _Biochem. J._, 32, 646 (1938). Article CAS Google Scholar * Keilin, D., and Hartree, E. F., _Nature_, 148, 75 (1941). Article ADS
CAS Google Scholar * Parpart, A. K., _J. Cell. and Comp. Physiol._, 19, 248 (1942). Article CAS Google Scholar * Steinhardt, J., _J. Biol. Chem._, 123, 543 (1938). CAS Google Scholar
Download references AUTHOR INFORMATION AUTHORS AND AFFILIATIONS * Department of Medicine, Columbia University College of Physicians and Surgeons, HELEN M. ANDERSON & JOSEPH C. TURNER *
the Presbyterian Hospital, New York HELEN M. ANDERSON & JOSEPH C. TURNER Authors * HELEN M. ANDERSON View author publications You can also search for this author inPubMed Google Scholar
* JOSEPH C. TURNER View author publications You can also search for this author inPubMed Google Scholar RIGHTS AND PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE THIS ARTICLE
ANDERSON, H., TURNER, J. Preparation and the Hæmoglobin Content of Red Cell ‘Ghosts’. _Nature_ 183, 112–113 (1959). https://doi.org/10.1038/183112a0 Download citation * Issue Date: 10
January 1959 * DOI: https://doi.org/10.1038/183112a0 SHARE THIS ARTICLE Anyone you share the following link with will be able to read this content: Get shareable link Sorry, a shareable link
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