**4. Glycoproteins of teleost RBC membranes**

We examined the GPs in the RBCs of carp (**Figure 3** Lane 6), yellow tail and red sea bream (**Figure 4** Lanes 3 and 6) by SDS–PAGE under the same conditions as the human preparation, followed by staining with PAS reagent.

The PAS-stained bands in all teleost preparations were stained poorly in the same way as avian GPs [34]. The carp and yellow tail RBC membrane preparations yielded one major band on the SDS-gels (**Figures 3** Lane 6 and **4** Lane 3). The PAS stain pattern on the SDS-gels suggests that the carp and yellow tail RBC membranes had fewer forms of GP than the human RBC membrane. The main carp GP was located near the position of the carp and human band-3 proteins. In addition, the main carp GP was positioned near human GP A (dimer).

In the red sea bream, one major band and a faint band with lower molecular weight were observed (**Figure 4** Lane 6). Aoki et al. [35] detected some GP bands in rainbow trout preparation. There was one major band and two faint bands with lower molecular weights were detected. It was presumed that the major band was the GP dimer, while the faint band beneath the major band and the faint band with lower molecular weight were the incomplete polymer and monomer forms respectively. It is suggested that the major band in the red sea bream was a polymer form.

While membrane protein patterns (CBC-stained band patterns) are generally similar to those in humans, GP patterns (PAS-stained band patterns) are different in humans. These differences are caused by the components containing sialo-oligosaccharides.
