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 Analysis of Receptor for Vibrio choleraeEl Tor Hemolysin with a Monoclonal Antibody That Recognizes Glycophorin B of Human Erythrocyte Membrane

1999 ◽  
Vol 67 (10) ◽  
pp. 5332-5337 ◽  
Author(s):  
Dongyan Zhang ◽  
Junko Takahashi ◽  
Taiko Seno ◽  
Yoshihiko Tani ◽  
Takeshi Honda
Keyword(s):  
Monoclonal Antibody ◽  
Vibrio Cholerae ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Mammalian Cells ◽  
Biochemical Characterization ◽  
Human Erythrocytes ◽  
Human Erythrocyte Membrane ◽  
El Tor ◽  
Glycophorin B

ABSTRACT El Tor hemolysin (ETH), a pore-forming toxin secreted byVibrio cholerae O1 biotype El Tor and most Vibrio cholerae non-O1 isolates, is able to lyse erythrocytes and other mammalian cells. To study the receptor for this toxin or the related molecule(s) on erythrocyte, we first isolated a monoclonal antibody, B1, against human erythrocyte membrane, which not only blocks the binding of ETH to human erythrocyte but also inhibits the hemolytic activity of ETH. Biochemical characterization and immunoblotting revealed that this antibody recognized an epitope on the extracellular domain of glycophorin B, a sialoglycoprotein of erythrocyte membrane. Erythrocytes lacking glycophorin B but not glycophorin A were less sensitive to the toxin than were normal human erythrocytes. These results indicate that glycophorin B is a receptor for ETH or at least an associated molecule of the receptor for ETH on human erythrocytes.

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

Uptake and binding of disaccharides in human erythrocytes

1976 ◽  
Vol 54 (1) ◽  
pp. 99-101 ◽  
Author(s):  
Ivan Beneš ◽  
Arnošt Kotyk
Keyword(s):  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Intact Cell ◽  
Binding Capacity ◽  
Human Erythrocytes ◽  
Human Erythrocyte Membrane ◽  
Maximum Binding Capacity

Disaccharides (sucrose, lactose, melibiose, cellobiose, trehalose, maltose, and isomaltose) are not transported across the human erythrocyte membrane. Maltose alone is bound in appreciable amounts to the intact cell as well as ghost membranes and competes mutually for uptake with D-glucose. In (NH4)2SO4-precipitated membrane preparations, maltose binds more strongly than other disaccharides (KD = 1.3 × 10−5 M; maximum binding capacity, 71 pmol/mg protein) and again competes mutually with D-glucose. Phloretin inhibits the binding of glucose much more than that of maltose.

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 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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