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(Received for publication, December 12, 1995, and in revised form, March 20, 1996)
From the We have used rabbit polyclonal antisera raised
against synthetic peptides complementary to different domains of the Rh
polypeptides and Rh glycoprotein to examine the topography and
organization of these proteins in the human erythrocyte membrane.
Previously unrecognized exofacial protease sites have been identified
on Rh CcEe, D proteins, and Rh glycoprotein. The Rh D protein has two
specific bromelain cleavage sites located within the first and sixth
predicted external domains, with the site of cleavage localized in the
sixth domain to lie between residues 353 and 354. All Rh polypeptide
species were found to be susceptible to cleavage with trypsin and
subtilisin within the first external domain of these proteins. The Rh
glycoprotein has two bromelain cleavage sites within the first external
domain. These flank the single N-glycosylation site
(Asn37), with the cleavage site toward the C-terminal side
of this residue being between residues 39 and 40. Bromelain treatment
was found to deglycosylate the Rh glycoprotein. Immunoprecipitation
experiments have revealed that anti-C, -c,E, -e, and -D immune
complexes are reactive with antisera raised against the fourth
predicted external loop of the Rh proteins and the C-terminal domain.
These data indicate that the hypothesis that suggests Rh C/c antigens
are expressed on truncated Rh polypeptides by a mechanism of alternate
splicing is incorrect and support the hypothesis that Rh Cc and Ee
antigens are expressed on a single polypeptide chain.
Volume 271, Number 24,
Issue of June 14, 1996
pp. 14233-14239
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
§
,
,§
,
International Blood Group Reference
Laboratory, Southmead Rd., Southmead, Bristol BS10 5ND, the
§ Bristol Institute for Transfusion Sciences, Southmead Rd.,
Southmead, Bristol BS10 5ND, the 
Faculty of Applied Sciences,
University of the West of England, Coldharbor Lane, Frenchay, Bristol
BS16 1QY, and the '' Department of Biochemistry, University of Bristol,
University Walk, Bristol BS8 1TD, United Kingdom
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