Reducible components in the proteins of human erythrocyte membrane.

In contrast to a previous report, no collagen or elastin-type cross-linked derived from lysine-aldehydes were detected in human erythrocyte membranes. The major reducible components of erythrocyte membranes were shown to be hexosyllysines. From their structure it is clear that these components cannot act as cross-links between the protein subunits of the membrane. The components were also shown to be present in varying proportions in human serum albumin and haemoglobin. Whether the hexose attachments have any physiological significance or are artefacts of the analytical procedure has not yet been demonstrated. One other major reducible component was present but, although unidentified, this compound was shown to be unrelated to any of the known lysine-aldehyde-derived cross-links of collagen and elastin. A minor acidic component was identified as glucosylvaline derived from the N-terminus of the beta chain of haemoglobin A1c and not a lysine-aldehyde precursor of the collagen cross-links.