1975
DOI: 10.1016/0005-2795(75)90245-7
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Circular dichroism of erythrocyte membrane glycoproteins

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1976
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Cited by 7 publications
(2 citation statements)
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“…Both glycophorin A and neuraminidase-treated glycophorin A, termed desialylglycophorin A, show very similar CD spectra. This is consistent with previous findings, although we succeeded in removing more than 90% of the sialic acid from the glycoprotein rather than the 60% previously reported (Decker & Carraway, 1975). Some differences in the spectra appear in the wavelength region below 220 nm, and these differences cause a slight change in the estimates of protein conformation.…”
Section: Resultssupporting
confidence: 92%
“…Both glycophorin A and neuraminidase-treated glycophorin A, termed desialylglycophorin A, show very similar CD spectra. This is consistent with previous findings, although we succeeded in removing more than 90% of the sialic acid from the glycoprotein rather than the 60% previously reported (Decker & Carraway, 1975). Some differences in the spectra appear in the wavelength region below 220 nm, and these differences cause a slight change in the estimates of protein conformation.…”
Section: Resultssupporting
confidence: 92%
“…Bovine rhodopsin in situ in the rod outer segment disk membranes yielded a helical content of about 29% by the same method of estimation (C. Rafferty and J. Y. Cassim, manuscript in preparation). For comparison, the helical contents of non-photosensitive membrane proteins in situ were also estimated by this procedure utilizing previously published membrane CD parameters (35,(41)(42)(43). In all cases for which CD data was available the helical content was less than those obtained for the bacteriorhodopsin in situ.…”
Section: Far Ultraviolet Spectramentioning
confidence: 99%