scholarly journals Isolation of cDNA clones for human erythrocyte membrane sialoglycoproteins α and δ

1988 ◽  
Vol 254 (3) ◽  
pp. 743-750 ◽  
Author(s):  
C G Tate ◽  
M J A Tanner
Keyword(s):  
Amino Acid ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Peptide Sequencing ◽  
Predicted Amino Acid Sequence ◽  
Cdna Clones ◽  
Amino Acid Residues ◽  
Human Erythrocyte Membrane ◽  
Cdna Sequences ◽  
Strong Homology

We have isolated almost full-length cDNA clones corresponding to human erythrocyte membrane sialoglycoproteins alpha (glycophorin A) and delta (glycophorin B). The predicted amino acid sequence of delta differs at two amino acid residues from the sequence determined by peptide sequencing. The sialoglycoprotein delta clone we have isolated contains an interrupting sequence within the region that gives rise to the cleaved N-terminal leader sequence for the protein and represents a product that is unlikely to be inserted into the erythrocyte membrane. Comparison of the cDNA sequences of alpha and delta shows very strong homology at the DNA level within the coding regions. The two mRNA sequences are closely related and differ by a number of clearly defined insertions and deletions.

scholarly journals Isolation of cDNA clones for a 50 kDa glycoprotein of the human erythrocyte membrane associated with Rh (rhesus) blood-group antigen expression

1992 ◽  
Vol 287 (1) ◽  
pp. 223-228 ◽  
Author(s):  
K Ridgwell ◽  
N K Spurr ◽  
B Laguda ◽  
C MacGeoch ◽  
N D Avent ◽  
...  
Keyword(s):  
Amino Acid ◽  
Membrane Proteins ◽  
Amino Acid Sequence ◽  
Blood Group ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Cdna Clones ◽  
Blood Group Antigens ◽  
Human Erythrocyte Membrane ◽  
Degenerate Primers

The Rh blood-group antigens are associated with human erythrocyte membrane proteins of approx. 30 kDa (the Rh30 polypeptides). Heterogeneously glycosylated membrane proteins of 50 and 45 kDa (the Rh50 glycoproteins) are coprecipitated with the Rh30 polypeptides on immunoprecipitation with anti-Rh-specific mono- and poly-clonal antibodies. We have isolated cDNA clones representing a member of the Rh50 glycoprotein family (the Rh50A glycoprotein). We used PCR with degenerate primers based on the N-terminal amino acid sequence of the Rh50 glycoproteins and human genomic DNA as a template and cloned and sequenced three types of PCR product of the expected size. Two of these products, Rh50A and Rh50B, gave the same translated amino acid sequence which corresponded to the expected Rh50 glycoprotein sequence but had only 75% DNA sequence similarity. The third product (Rh50C) contained a single base deletion, and the translated amino acid sequence contained an in-frame stop codon. We have isolated cDNA clones containing the full coding sequence of the Rh50A glycoprotein. This sequence predicts that it is a 409-amino acid N-glycosylated membrane protein with up to 12 transmembrane domains. The Rh50A glycoprotein shows clear similarity to the Rh30A protein in both amino acid sequence and predicted topology. Our results are consistent with the Rh30 and Rh50 groups of proteins being different subunits of an oligomeric complex which is likely to have a transport or channel function in the erythrocyte membrane. We mapped the Rh50A gene to human chromosome 6p21-qter, showing that genetic differences in the Rh30 rather than the Rh50 genes specify the major polymorphic forms of the Rh antigens.

scholarly journals Human erythrocyte membrane sialoglycoprotein β. The cDNA sequence suggests the absence of a cleaved N-terminal signal sequence

1987 ◽  
Vol 243 (1) ◽  
pp. 277-280 ◽  
Author(s):  
S High ◽  
M J A Tanner
Keyword(s):  
Membrane Protein ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Cdna Sequence ◽  
Signal Sequence ◽  
Human Kidney ◽  
Cdna Clones ◽  
Erythroid Cells ◽  
Coding Region ◽  
Human Erythrocyte Membrane

We have isolated cDNA clones corresponding to the human erythrocyte membrane sialoglycoprotein beta. The clones encompass the coding region for the protein, 120 residues of the 5′ non-coding region and the 3′ non-coding region. The cDNA sequence suggests that sialoglycoprotein beta is not translated with the cleaved N-terminal signal sequence usual in a membrane protein of this type. Sialoglycoprotein beta or a closely related homologue is present in human kidney as well as erythroid cells.

scholarly journals Mapping of a palmitoylatable band 3-binding domain of human erythrocyte membrane protein 4.2

1999 ◽  
Vol 340 (2) ◽  
pp. 505-512 ◽  
Author(s):  
Raja BHATTACHARYYA ◽  
Amit K. DAS ◽  
Prasun K. MOITRA ◽  
Biswajit PAL ◽  
Indranil MANDAL ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Band 3 ◽  
Amino Acid Residues ◽  
Fusion Peptides ◽  
Human Erythrocyte Membrane ◽  
Erythrocyte Membrane Protein ◽  
Protein 4.2 ◽  
Positive Modulator

Evidence accumulated over the years suggests that human erythrocyte membrane protein 4.2 is one of the proteins involved in strengthening the cytoskeleton-membrane interactions in the red blood cell. Deficiency of protein 4.2 is linked with a variety of hereditary haemolytic anaemia. However, the interactions of protein 4.2 with other proteins of the erythrocyte membrane remain poorly understood. The major membrane-binding site for protein 4.2 resides on the cytoplasmic domain of band 3 (CDB3). In order to carry out an initial characterization of its interaction with the CDB3, protein 4.2 was subjected to proteolytic cleavage and gel renaturation assay, and the 23-kDa N-terminal domain was found to interact with band 3. This domain contained two putative palmitoylatable cysteine residues, of which cysteine 203 was identified as the palmitoylatable cysteine. Recombinant glutathione S-transferase-fusion peptides derived from this domain were characterized with respect to their ability to interact with the CDB3. Whereas these studies do not rule out the involvement of other subsites on protein 4.2 in interaction with the CDB3, the evidence suggests that the region encompassing amino acid residues 187-211 is one of the domains critical for the protein 4.2-CDB3 interaction. This is also the first demonstration that palmitoylation serves as a positive modulator of this interaction.

Amino Acid Sequence of the Blood Group Mg-Specific Major Human Erythrocyte Membrane Sialoglycoprotein

1981 ◽  
Vol 362 (1) ◽  
pp. 81-86 ◽  
Author(s):  
Wolfgang DAHR ◽  
Konrad BEYREUTHER ◽  
Ernst GALLASCH ◽  
Jürgen KRÜGER ◽  
Phyllis MOREL
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Blood Group ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Human Erythrocyte Membrane

Molecular cloning and hormonal control in the ovary of connexin 31.5 mRNA and correlation with the appearance of oocyte maturational competence in red seabream

2000 ◽  
Vol 203 (21) ◽  
pp. 3299-3306
Author(s):  
C.Y. Choi ◽  
F. Takashima
Keyword(s):  
Amino Acid ◽  
Hormonal Control ◽  
Predicted Amino Acid Sequence ◽  
Amino Acid Residues ◽  
Reading Frame ◽  
Red Seabream ◽  
Consensus Sequences ◽  
Cdna Sequences ◽  
Connexin Gene ◽  
Connexin Genes

Gap junctions are aggregates of intercellular channels, composed of the protein connexin (Cx), between adjacent cells. This study examined whether, in the ovary of the red seabream Pagrus major, the connexin gene essential for the production of RNA and protein during the acquisition of oocyte maturational competence is active. Mixed primers for this reaction were designed on the basis of the high sequence homology of selected regions of known connexin genes. Polymerase-chain-reaction-amplified cDNA fragments generated by 3′ and 5′ rapid amplication of cDNA ends were combined to generate full-length cDNA sequences. The resulting 2400 base pair cDNA had an open reading frame encoding a polypeptide containing 275 amino acid residues (31493 Da; Cx31.5). Hydropathicity analysis of the predicted amino acid sequence indicated that red seabream Cx31.5 has four major hydrophobic regions and four major hydrophilic regions indicative of a topology similar to that of known connexins. Typical connexin consensus sequences were also observed in the first and second extracellular loops. During the acquisition of oocyte maturational competence, red seabream Cx31.5 mRNA transcription levels increased after treatment with gonadotropin-II. It is therefore proposed that expression of Cx31.5 contributes to the acquisition of oocyte maturational competence in this species.

scholarly journals Facilitated transport of amino acids across organic phases and the human erythrocyte membrane

1980 ◽  
Vol 188 (2) ◽  
pp. 541-548 ◽  
Author(s):  
R C Hider ◽  
W McCormack
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Erythrocyte Membrane ◽  
Transfer Process ◽  
Human Erythrocyte ◽  
Facilitated Transport ◽  
Human Erythrocytes ◽  
Human Erythrocyte Membrane ◽  
Chloroform Phase

1. An artificial facilitated amino-acid-transfer process operating across a chloroform phase is reported. 2. This process utilizes a family of bis(salicylamidato)copper(II) complexes. 3. A mechanism is proposed for this process and for its sensitivity towards cyanide and bathophenanthroline sulphonate. 4. Facilitated transfer of L-leucine in human erythrocytes has been shown to be inhibited by bathophenanthroline sulphonate.

scholarly journals Amino acid sequence of the N alpha-terminal 201 residues of human erythrocyte membrane band 3.

1983 ◽  
Vol 258 (13) ◽  
pp. 7981-7990 ◽  
Author(s):  
R K Kaul ◽  
S N Murthy ◽  
A G Reddy ◽  
T L Steck ◽  
H Kohler
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Band 3 ◽  
Human Erythrocyte Membrane
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