PMID- 1059087
OWN - NLM
STAT- MEDLINE
DCOM- 19760116
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 72
IP  - 8
DP  - 1975 Aug
TI  - Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte
      glycophorin.
PG  - 2964-8
AB  - Glycophorin, the major sialoglycoprotein of the human erythrocyte membrane, is
      composed of 131 amino acids and an average of 16 oligosaccharide chains. Fifteen 
      oligosaccharides are linked to threonine/serine residues via O-glycosidic bonds, 
      and one more complex unit is attached to asparagine. The location of each of
      these oligosaccharides and the complete amino-acid sequence of this molecular
      have been determined by Edman degradation techniques. Glycophorin appears to be
      organized into three distinct "domains" on the basis of the locations of
      glycosylated amino acids and the clustering of residues of similar type. These
      include (i) a glycosylated segment composed of approximately 64 residues from the
      NH2-terminus, (ii) a "hydrophobic" segment of approximately 32 nonpolar residues,
      and (iii) a COOH-terminal segment, composed of approximately 35 residues, which
      has an unusual concentration of hydrophilic amino acids. This unique structure is
      consistent with the earlier suggestions that glycophorin is one of the major
      "intrinsic" membrane proteins which has a transmembrane orientation.
FAU - Tomita, M
AU  - Tomita M
FAU - Marchesi, V T
AU  - Marchesi VT
LA  - eng
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Amino Acids)
RN  - 0 (Blood Proteins)
RN  - 0 (Glycoproteins)
RN  - 0 (Hexoses)
RN  - 0 (Macromolecular Substances)
RN  - 0 (Oligosaccharides)
RN  - 0 (Sialic Acids)
SB  - IM
MH  - Amino Acids/analysis
MH  - Binding Sites
MH  - Blood Proteins/*analysis
MH  - Erythrocytes/*analysis
MH  - Glycoproteins/*analysis
MH  - Hexoses/analysis
MH  - Humans
MH  - Macromolecular Substances
MH  - Molecular Weight
MH  - Oligosaccharides/analysis
MH  - Protein Binding
MH  - Sialic Acids/analysis
PMC - PMC432899
EDAT- 1975/08/01 00:00
MHDA- 1975/08/01 00:01
CRDT- 1975/08/01 00:00
PHST- 1975/08/01 00:00 [pubmed]
PHST- 1975/08/01 00:01 [medline]
PHST- 1975/08/01 00:00 [entrez]
AID - 10.1073/pnas.72.8.2964 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1975 Aug;72(8):2964-8. doi: 10.1073/pnas.72.8.2964.