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  • 1
    Electronic Resource
    Electronic Resource
    Magnetic circular dichroism of Na3Nd(ODA)3⋅2NaClO4⋅6H2O (1996)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 105 (1996), S. 6117-6127 
    Details
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: This paper emphasizes the complementarity between optical and magneto-optical measurements on f elements. The magnetic circular dichroism, circular dichroism, and polarized absorption spectra of Na3Nd(ODA)3⋅2NaClO4⋅6H2O (NdODA), have been recorded at 4.2 K between 5000 and 30 000 cm−1. The electric dipole contributions to the f–f transitions are analyzed using a parametric model which contains 12 parameters which are determined by fitting the calculated to the empirical dipole strengths of 50 α and 16 π polarized absorption lines. The reliability of these intensity parameters is tested by simulating the more sensitive magneto-optical (magnetic circular dichroism) and chiroptical (circular dichroism) spectra. © 1996 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.472471
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Propagation of a picosecond-duration, relativistic electron beam through hydrogen at atmospheric pressures (1988)
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 64 (1988), S. 575-580 
    Details
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: An experiment demonstrating the propagation of a 42-MeV electron beam from an rf linear accelerator through 1 m of H2 at pressures from 10−3 to 1.25 atm is reported. Measurements were made of the transmitted current and the beam's radius, transverse position, and angular divergence along the path. The beam current was fully transmitted at all pressures, without the often detrimental plasma interactions (space-charge neutralization, magnetic neutralization, and various plasma instabilities) seen in previous studies. The observed beam expansion was consistent with calculations of multiple scattering. The propagation can be attributed to the 4-ps duration of the accelerator's electron bunches. This time is three to four orders of magnitude shorter than that used in the earlier work and is shorter than the growth times for the beam-plasma interactions. Such a beam should prove suitable for a gas-loaded free-electron laser.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.341972
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  • 3
    Electronic Resource
    Electronic Resource
    Non-Hermitian perturbative effective operators: Connectivity and derivation of diagrammatic representation (2001)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 115 (2001), S. 8279-8284 
    Details
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: Effective Hamiltonians and effective operators act on a restricted model space to give the same energies and matrix elements as those of the full Hamiltonian and operators between the corresponding true eigenstates. For the effective Hamiltonian there are two "obvious" choices: the simplest non-Hermitian effective Hamiltonian and the canonical Hermitian effective Hamiltonian. In this paper, we derive a perturbative effective operator which works together with the non-Hermitian effective Hamiltonian, prove that it can be expanded with only connected diagrams, and show how to construct the connected diagrams easily from the diagrams of the effective Hamiltonian by substitution of vertices. This effective operator is much simpler than the Hermitian effective operator and therefore is expected to be more suitable for ab initio calculations. © 2001 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.1408300
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  • 4
    Electronic Resource
    Electronic Resource
    Analysis of the crystal-field spectra of the actinide tetrafluorides. I. UF4, NpF4, and PuF4 (1991)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 95 (1991), S. 7194-7203 
    Details
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: An interpretation of the low-temperature absorption spectra of AnF4 (An=U, Np, Pu) is presented. Using an effective operator Hamiltonian with orthogonalized free-ion operators and initializing crystal-field parameter values based on a superposition model calculation for An4+ sites with C2 symmetry, good agreement between the model calculations and experimentally observed absorption band structure could be obtained. Correlations with published magnetic and heat capacity measurements are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.461396
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  • 5
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    Topology of Kell blood group protein and the expression of multiple antigens by transfected cells (1994)
    American Society of Hematology
    Details
    Publication Date: 1994-11-15
    Description: Kell is one of the major blood group systems in human red blood cells (RBCs). The Kell antigens are carried on a 731 amino acid glycoprotein that is thought to span the erythrocyte membrane once. Rabbit antibodies to three synthetic peptides, derived from different parts of the Kell protein, were used to determine the topology of Kell protein on the RBC. Antibodies to a C-terminal peptide and to a peptide derived from amino acid residues 410 to 439 reacted with RBCs treated with 0.2 mol/L dithiothreitol. An antibody to the N-terminal peptide reacted with inside-out RBC vesicles but not with right-side-out vesicles nor with intact RBCs, showing that Kell is a type II membrane protein and that the extracellular portion of the protein is folded by disulfide bonds. By transfection, Kell protein was expressed on the cell surface of surrogate cells, and the transfected cells expressed similar antigenic properties as native RBCs. Kell protein was expressed in COS- 1 and K562 cells and in Sf9 cells infected by the Baculovirus system. Transfected K562 cells expressed several high-incidence antigens but not the low-incidence antigen K1.
    Print ISSN: 0006-4971
    Electronic ISSN: 1528-0020
    Topics: Biology , Medicine
    Published by American Society of Hematology
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  • 6
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    Molecular analysis of glycophorin C deficiency in human erythrocytes (1993)
    American Society of Hematology
    Details
    Publication Date: 1993-05-15
    Description: Human erythrocyte glycophorin C plays a functionally important role in maintaining erythrocyte shape and regulating membrane mechanical stability. We report here the characterization of the glycophorins C and D deficiency in erythrocytes of the Leach phenotype. Glycophorin C gene is encoded by 4 exons. Amplification of reticulocyte cDNA from Leach phenotype and normal individuals generated a 140-bp fragment when using primers spanning exons 1 and 2. However, no polymerase chain reaction (PCR) products were detected in the Leach phenotype using primers flanking either exons 1 and 3 or exons 1 and 4, suggesting that the 3' end of the mRNA was missing or altered. Exon 4 also appeared to be missing from Leach genomic DNA, based on both Southern hybridization and PCR. These results indicate that an absence of glycophorin C and glycophorin D in erythrocytes from these Leach phenotype individuals is a consequence of a deletion or marked alteration of exon 3 and exon 4 of their glycophorin C gene. Surprisingly, the mutant gene encodes an mRNA stable enough to be detected in circulating reticulocytes. Although this mRNA could encode an N-terminal fragment of glycophorin C, these protein isoform(s) would not be expressed in the membrane because they lack the transmembrane and cytoplasmic domains.
    Print ISSN: 0006-4971
    Electronic ISSN: 1528-0020
    Topics: Biology , Medicine
    Published by American Society of Hematology
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  • 7
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    Molecular analysis of glycophorin C deficiency in human erythrocytes (1993)
    American Society of Hematology
    Details
    Publication Date: 1993-05-15
    Description: Human erythrocyte glycophorin C plays a functionally important role in maintaining erythrocyte shape and regulating membrane mechanical stability. We report here the characterization of the glycophorins C and D deficiency in erythrocytes of the Leach phenotype. Glycophorin C gene is encoded by 4 exons. Amplification of reticulocyte cDNA from Leach phenotype and normal individuals generated a 140-bp fragment when using primers spanning exons 1 and 2. However, no polymerase chain reaction (PCR) products were detected in the Leach phenotype using primers flanking either exons 1 and 3 or exons 1 and 4, suggesting that the 3' end of the mRNA was missing or altered. Exon 4 also appeared to be missing from Leach genomic DNA, based on both Southern hybridization and PCR. These results indicate that an absence of glycophorin C and glycophorin D in erythrocytes from these Leach phenotype individuals is a consequence of a deletion or marked alteration of exon 3 and exon 4 of their glycophorin C gene. Surprisingly, the mutant gene encodes an mRNA stable enough to be detected in circulating reticulocytes. Although this mRNA could encode an N-terminal fragment of glycophorin C, these protein isoform(s) would not be expressed in the membrane because they lack the transmembrane and cytoplasmic domains.
    Print ISSN: 0006-4971
    Electronic ISSN: 1528-0020
    Topics: Biology , Medicine
    Published by American Society of Hematology
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  • 8
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    Topology of Kell blood group protein and the expression of multiple antigens by transfected cells (1994)
    American Society of Hematology
    Details
    Publication Date: 1994-11-15
    Description: Kell is one of the major blood group systems in human red blood cells (RBCs). The Kell antigens are carried on a 731 amino acid glycoprotein that is thought to span the erythrocyte membrane once. Rabbit antibodies to three synthetic peptides, derived from different parts of the Kell protein, were used to determine the topology of Kell protein on the RBC. Antibodies to a C-terminal peptide and to a peptide derived from amino acid residues 410 to 439 reacted with RBCs treated with 0.2 mol/L dithiothreitol. An antibody to the N-terminal peptide reacted with inside-out RBC vesicles but not with right-side-out vesicles nor with intact RBCs, showing that Kell is a type II membrane protein and that the extracellular portion of the protein is folded by disulfide bonds. By transfection, Kell protein was expressed on the cell surface of surrogate cells, and the transfected cells expressed similar antigenic properties as native RBCs. Kell protein was expressed in COS- 1 and K562 cells and in Sf9 cells infected by the Baculovirus system. Transfected K562 cells expressed several high-incidence antigens but not the low-incidence antigen K1.
    Print ISSN: 0006-4971
    Electronic ISSN: 1528-0020
    Topics: Biology , Medicine
    Published by American Society of Hematology
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  • 9
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    Molecular basis of the Kell (K1) phenotype (1995)
    American Society of Hematology
    Details
    Publication Date: 1995-02-15
    Description: K1 (K, Kell) is a strong immunogen; its antibodies can cause severe reactions if incompatible blood is transfused and may cause hemolytic disease of the newborn in sensitized mothers. K1 is a member of the Kell blood group system, which is complex, containing over 20 different antigens. Some of the antigens are organized in allelic pairs of high and low prevalence whereas others are independently expressed. K1, which is present in 9% of the population, is antithetical to the high- prevalence K2 (k) antigen. We have determined the molecular basis of the K1/K2 polymorphism by sequencing the 19 exons of the Kell gene (KEL) of a K1/K1 person. Polymerase chain reaction was performed on genomic DNA isolated from peripheral blood and the amplified products were either directly sequenced or subcloned and sequenced. Comparisons of K1/K1 and K2/K2 DNA showed a C to T base substitution in exon 6 that predicts a threonine to methionine change at amino acid residue 193. This amino acid substitution occurs at a consensus N-glycosylation site (Asn. X. Thr) and probably prevents N-glycosylation, leading to a change in phenotype. The C to T substitution creates a Bsm I restriction enzyme site, which was tested in 42 different samples to confirm that this base change identifies the K1/K1 genotype. This test differentiates genotypes, K1/K1, K2/K2, and the K1/K2 heterozygote and should prove useful in the prenatal diagnosis of K1-related hemolytic disease of the newborn.
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    Electronic ISSN: 1528-0020
    Topics: Biology , Medicine
    Published by American Society of Hematology
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  • 10
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    A point mutation in the GYPC gene results in the expression of the blood group Ana antigen on glycophorin D but not on glycophorin C: further evidence that glycophorin D is a product of the GYPC gene (1993)
    American Society of Hematology
    Details
    Publication Date: 1993-11-15
    Description: Glycophorin C (GPC) and glycophorin D (GPD) are homologous sialoglycoproteins in the human red blood cell membrane. Both are thought to be encoded by the GPC gene (GYPC). We report that the rare blood group antigen, Ana, is expressed on GPD but not on GPC. cDNA was synthesized from total RNA obtained from two unrelated, heterozygous Ana+ blood donors and analyzed by the polymerase chain reaction using primers that spanned sequences encoded by the GYPC gene. The expected 412-bp fragment was generated, and sequencing of the amplified product showed a G--〉T substitution at nucleotide 67 of the coding sequence, resulting in the substitution of alanine by serine at amino acid residue 23 of GPC and, presumably, residue 2 of GPD. To explain the expression of Ana on GPD but not on GPC, we postulate that the conformation of the amino acid residues at the N-terminal region of GPD determines the antigenic expression as this conformation would be different from that of the same sequence of amino acids occurring within GPC. Other possible reasons for antigen expression on a shorter protein product but not on the full-length protein product of the same gene are discussed. We extrapolate this reasoning to account for the expression of the common GE2 blood group antigen on GPD but not on GPC.
    Print ISSN: 0006-4971
    Electronic ISSN: 1528-0020
    Topics: Biology , Medicine
    Published by American Society of Hematology
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