Structural homology between glycophorins C and D of human erythrocytes
Open Access
- 1 August 1989
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 183 (3) , 639-643
- https://doi.org/10.1111/j.1432-1033.1989.tb21093.x
Abstract
Glycophorin C (GPC) and D (GPD) are minor glycoproteins which are believed to be important for the structural integrity of the red cell membrane. We have investigated the structural relationship between these glycoproteins by both immunological and structural investigations: 1 A rabbit anti-serum produced against GPD reacts strongly with GPC and the abnormal glycoproteins of Gerbich: –2, –3 and Gerbich: –2,3 red cells, and recognizes most probably the homologous C-terminal portions of GPC and GPD. The two molecules however differ at their N-terminus. 2 One-dimensional mapping of the peptides obtained after tryptic, chymotryptic, V8 protease or acid cleavage of 125 I-labelled GPC and GPD, indicated that GPC and GPD are structurally related but some differences were found indicating that additional peptides were generated from GPC. 3 The partial primary structure of GPD was determined. The sequencing data are consistent with the assumption that GPD represents an abridged version of GPC that comprises residues approximately 21/29–128 and exhibits a N-terminal residue that is blocked by an as yet undefined group.This publication has 33 references indexed in Scilit:
- High Frequency Antigens of Human Erythrocyte Membrane Sialoglycoproteins, V.Characterization of the Gerbich Blood Group Antigens: Ge2 and Ge3Biological Chemistry Hoppe-Seyler, 1987
- A Family Demonstrating Inheritance of the Leach Phenotype: a Gerbich‐Negative Phenotype Associated with ElliptocytosisVox Sanguinis, 1986
- Altered Membrane Sialoglycoproteins in Human Erythrocytes Lacking the Gerbich Blood Group AntigensBiological Chemistry Hoppe-Seyler, 1985
- N‐Terminal Amino Acid Sequence of Sialoglycoprotein D (Glycophorin C) from Human Erythrocyte MembranesEuropean Journal of Biochemistry, 1982
- Structure of the Ss Blood Group Antigens, II. A Methionine/Threonine Polymorphism within the N-terminal Sequence of the Ss GlycoproteinHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1980
- Structure of the Ss Blood Group Antigens. I. Isolation of Ss-Active Glycopeptides and Differentiation of the Antigens by Modification of MethionineHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1980
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- Micro‐sequence analysis of peptides and proteins using 4‐NN‐dimethylaminoazobenzene 4′‐isothiocyanate/phenylisothiocyanate double coupling methodFEBS Letters, 1978
- Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a,6a-diphenylglycolurilBiochemical and Biophysical Research Communications, 1978
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970