The Experts below are selected from a list of 51633 Experts worldwide ranked by ideXlab platform
Shanjing Yao - One of the best experts on this subject based on the ideXlab platform.
-
adsorption characteristics of Human Immunoglobulin g on five new tetrapeptide biomimetic affinity resins
Journal of Chemical & Engineering Data, 2019Co-Authors: Hongyun Zhu, Shenggang Chen, Qilei Zhang, Dongqiang Lin, Shanjing YaoAbstract:Alternative antibody-binding affinity ligands are expected to support robust time- and cost-effective antibody purification with rapid improvement of upstream productivity and demand on downstream process optimization. Five new tetrapeptide biomimetic affinity ligands (FYRH, HWRH, YHRI, HYRF, and FHRA) were screened by modeling the molecular interaction mechanism between tetrapeptide ligands and the Fc fragment of IgG with molecular dynamics simulation and the flexible docking method, and the corresponding five resins were prepared in this work to evaluate their adsorption characteristics of Human Immunoglobulin G (hIgG). The results showed that the binding capacities to hIgG of the five resins showed a strong pH-dependency, which was high at pH 7.0–9.0, and extremely low at pH 5.0–6.0, providing a benefit choice to separate hIgG. The dynamic binding capacities (DBC) at 10% breakthrough of five resins could reach up to 28–37 mg/mLgel, and Ac-FYRH-4FF resin showed the best adsorption performance. The eluti...
-
coadsorption of Human Immunoglobulin g and bovine serum albumin on a p aminohippuric acid based mixed mode resin
Journal of Chemical & Engineering Data, 2016Co-Authors: Jun Yan, Qilei Zhang, Dongqiang Lin, Shanjing YaoAbstract:Mixed-mode chromatography (MMC) has been developed as a cost-effective new technique for antibody purification. Nuvia cPrime (NP) is a novel MMC resin with p-aminohippuric acid as the functional ligand. The adsorption of Human Immunoglobulin G (IgG) and bovine serum albumin (BSA) on NP was measured, including single component adsorption at different pH and binary coadsorption at various pH values and IgG/BSA mass ratios. Typical pH-dependent adsorption behavior was found in the single component adsorption which can be described by a two-parameter equation that offered a convenient way to analyze pH effects. Moreover, a competitive and preferential adsorption of IgG to BSA was investigated in binary coadsorption. Extended Langmuir (EL) and Extended Langmuir−Freundlich (ELF) models with parameters obtained from single-component isotherms were used to describe the coadsorption behaviors of IgG and BSA at various mass ratios. The results indicated the ELF model was more suitable for IgG adsorption, while the ...
-
Coadsorption of Human Immunoglobulin G and Bovine Serum Albumin on a p‑Aminohippuric Acid Based Mixed-Mode Resin
2016Co-Authors: Jun Yan, Qilei Zhang, Dongqiang Lin, Shanjing YaoAbstract:Mixed-mode chromatography (MMC) has been developed as a cost-effective new technique for antibody purification. Nuvia cPrime (NP) is a novel MMC resin with p-aminohippuric acid as the functional ligand. The adsorption of Human Immunoglobulin G (IgG) and bovine serum albumin (BSA) on NP was measured, including single component adsorption at different pH and binary coadsorption at various pH values and IgG/BSA mass ratios. Typical pH-dependent adsorption behavior was found in the single component adsorption which can be described by a two-parameter equation that offered a convenient way to analyze pH effects. Moreover, a competitive and preferential adsorption of IgG to BSA was investigated in binary coadsorption. Extended Langmuir (EL) and Extended Langmuir−Freundlich (ELF) models with parameters obtained from single-component isotherms were used to describe the coadsorption behaviors of IgG and BSA at various mass ratios. The results indicated the ELF model was more suitable for IgG adsorption, while the EL model was better for describing the weak binding of BSA at pH 7.0 and 8.0
Fumihiko Matsuda - One of the best experts on this subject based on the ideXlab platform.
-
the Human Immunoglobulin heavy variable genes
Experimental and Clinical Immunogenetics, 1999Co-Authors: Nathalie Pallares, Fumihiko Matsuda, Valerie Contet, Mariepaule Lefranc, Sophie LefebvreAbstract:'Human Immunoglobulin Heavy Variable Genes', the fourth report of the 'IMGT Locus on Focus' section, comprises five tables entitled: (1) 'Number of Human germline IGHV genes at 14q32.33 and potential repertoire'; (2) 'Human germline IGHV genes at 14q32.33'; (3) 'Human IGHV orphons on chromosome 15 (15q11.2)'; (4) 'Human IGHV orphons on chromosome 16 (16p11.2)', and (5) 'Human IGHV allele table'. These tables are available at the IMGT Marie-Paule page from IMGT, the international ImMunoGeneTics database (http://imgt.cnusc.fr:8104) created by Marie-Paule Lefranc, Universite Montpellier II, CNRS, France.
-
the complete nucleotide sequence of the Human Immunoglobulin heavy chain variable region locus
Journal of Experimental Medicine, 1998Co-Authors: Fumihiko Matsuda, Kazuo Ishii, Patrice Bourvagnet, K Kuma, Hidenori Hayashida, Takashi Miyata, Tasuku HonjoAbstract:The complete nucleotide sequence of the 957-kb DNA of the Human Immunoglobulin heavy chain variable (VH) region locus was determined and 43 novel VH segments were identified. The region contains 123 VH segments classifiable into seven different families, of which 79 are pseudogenes. Of the 44 VH segments with an open reading frame, 39 are expressed as heavy chain proteins and 1 as mRNA, while the remaining 4 are not found in Immunoglobulin cDNAs. Combinatorial diversity of VH region was calculated to be ∼6,000. Conservation of the promoter and recombination signal sequences was observed to be higher in functional VH segments than in pseudogenes. Phylogenetic analysis of 114 VH segments clearly showed clustering of the VH segments of each family. However, an independent branch in the tree contained a single VH, V4-44.1P, sharing similar levels of homology to Human VH families and to those of other vertebrates. Comparison between different copies of homologous units that appear repeatedly across the locus clearly demonstrates that dynamic DNA reorganization of the locus took place at least eight times between 133 and 10 million years ago. One nonImmunoglobulin gene of unknown function was identified in the intergenic region.
-
structure and physical map of 64 variable segments in the 3 0 8 megabase region of the Human Immunoglobulin heavy chain locus
Nature Genetics, 1993Co-Authors: Fumihiko Matsuda, Euy Kyun Shin, Hitoshi Nagaoka, Ryusuke Matsumura, Makoto Haino, Yosho Fukita, Shigeo Takaishi, Takashi Imai, John H Riley, Rakesh AnandAbstract:Structure and physical map of 64 variable segments in the 3′ 0.8–megabase region of the Human Immunoglobulin heavy–chain locus
-
structure and physical map of 64 variable segments in the 3 0 8 megabase region of the Human Immunoglobulin heavy chain locus
Nature Genetics, 1993Co-Authors: Fumihiko Matsuda, Euy Kyun Shin, Hitoshi Nagaoka, Ryusuke Matsumura, Makoto Haino, Yosho Fukita, Shigeo Takaishi, Takashi Imai, John H Riley, Rakesh AnandAbstract:We have constructed the physical map of the 0.8 megabase DNA fragment which contains the 3' 64 variable region (V) gene segments of the Human Immunoglobulin heavy chain (H) locus. The organization of the VH locus showed several features that indicate dynamic reshuffling of this locus. The sequenced 64 VH segments include 31 pseudogenes, of which 24 are highly conserved except for a few point mutations. Comparison of the 64 germline VH sequences shows that each VH family has conserved sequences, suggesting that there might be some genetic or selection mechanisms involved in maintenance of each family. The total number of the Human VH segments was estimated to be about 120, including at least 7 orphons.
Mariepaule Lefranc - One of the best experts on this subject based on the ideXlab platform.
-
nomenclature of the Human Immunoglobulin lambda igl genes
Experimental and Clinical Immunogenetics, 2001Co-Authors: Mariepaule LefrancAbstract:'Nomenclature of the Human Immunoglobulin Lambda (IGL) Genes', the 18th report of the 'IMGT Locus in Focus' section, provides the first complete list of all the Human IGL genes. The total number of Human IGL genes per haploid genome is 87--96 (93--102 if the orphons are included), of which 37--43 genes are functional. IMGT/Human Genome Organization (HUGO) gene names and definitions of the Human IGL genes on chromosome 22q11.2 and IGL orphons on chromosomes 8 and 22 are provided with the gene functionality and the number of alleles, according to the rules of the IMGT Scientific chart, with the accession numbers of the IMGT reference sequences and with the accession ID of the Genome Database GDB and NCBI LocusLink databases, in which all the IMGT Human IGL genes have been entered. The tables are available at the IMGT Marie-Paule page of IMGT, the international ImMunoGeneTics database (http://imgt.cines.fr) created by Marie-Paule Lefranc, Universite Montpellier II, CNRS, France.
-
nomenclature of the Human Immunoglobulin heavy igh genes
Experimental and Clinical Immunogenetics, 2001Co-Authors: Mariepaule LefrancAbstract:'Nomenclature of the Human Immunoglobulin Heavy (IGH) Genes', the 16th report of the 'IMGT Locus in Focus' section, provides the first complete list of all the Human IGH genes. The total number of Human IGH genes per haploid genome is 170-176 (206-212 genes, if the orphons and the processed gene are included), of which 77-84 genes are functional. IMGT/Human Genome Organization (HUGO) gene names and definitions of the Human IGH genes on chromosome 14q32.33, processed gene on chromosome 9 and IGH orphons on chromosomes 15 and 16 are provided with the gene functionality and the number of alleles, according to the rules of the IMGT Scientific chart, with the accession numbers of the IMGT reference sequences and with the accession ID of the Genome Database GDB and NCBI LocusLink databases, in which all the IMGT Human IGH genes have been entered. The tables are available at the IMGT Marie-Paule page of IMGT, the international ImMunoGeneTics database (http://imgt.cines.fr:8104) created by Marie-Paule Lefranc, Universite Montpellier II, CNRS, France.
-
allelic polymorphisms and rflp in the Human Immunoglobulin lambda light chain locus
Human Genetics, 1999Co-Authors: Mariepaule Lefranc, Nathalie Pallares, Jeanpol FrippiatAbstract:The organization of the Human Immunoglobulin lambda light chain locus (IGL) was recently described. This locus has been entirely sequenced. To evaluate the extent of the genomic variability existing inside that locus, we compiled all the available sequences of germline IGLV genes to find variants of Vλ sequences. We also looked for RFLP polymorphisms in a reputedly highly polymorphic Human population from eastern Senegal, and compiled all RFLP data previously published. Analysis of these data indicates that IGLV alleles are frequent and increase the diversity of the lambda light chain repertoire in the Human population. In contrast, RFLP and polymorphism by insertion and/or deletion are limited in that locus. This observation reinforces our hypothesis that the Human IGL locus has undergone less evolutionary shuffling than the Human kappa or heavy-chain loci.
-
the Human Immunoglobulin heavy diversity ighd and joining ighj segments
Experimental and Clinical Immunogenetics, 1999Co-Authors: Manuel Ruiz, Nathalie Pallares, Valerie Contet, Valerie Barbie, Mariepaule LefrancAbstract:The ‘Human Immunoglobulin Heavy Diversity (IGHD) and Joining (IGHJ) segments’, fifth report of the ‘IMGT Locus on Focus’ section, comprises six tables entitled: (1) ‘Human germline IGHD segments at 14q32.33’; (2) ‘Human IGHD alleles’; (3) ‘Human germline IGHJ segments at 14q32.33’; (4) ‘Human IGHJ alleles’; (5) ‘Human germline IGHD orphons on chromosome 15 (15q11.2)’; (6) ‘Correspondence between the different Human IGHD nomenclatures’, and two figures: (1) ‘Protein display of Human IGH D-REGIONs’; (2) ‘Protein display of Human IGH J-REGIONs’. These tables and figures are available at the IMGT Marie-Paule page from IMGT, the international ImMunoGeneTics database (http://imgt.cnusc.fr:8104) created by Marie-Paule Lefranc, Universite Montpellier II, CNRS, France.
-
the Human Immunoglobulin heavy variable genes
Experimental and Clinical Immunogenetics, 1999Co-Authors: Nathalie Pallares, Fumihiko Matsuda, Valerie Contet, Mariepaule Lefranc, Sophie LefebvreAbstract:'Human Immunoglobulin Heavy Variable Genes', the fourth report of the 'IMGT Locus on Focus' section, comprises five tables entitled: (1) 'Number of Human germline IGHV genes at 14q32.33 and potential repertoire'; (2) 'Human germline IGHV genes at 14q32.33'; (3) 'Human IGHV orphons on chromosome 15 (15q11.2)'; (4) 'Human IGHV orphons on chromosome 16 (16p11.2)', and (5) 'Human IGHV allele table'. These tables are available at the IMGT Marie-Paule page from IMGT, the international ImMunoGeneTics database (http://imgt.cnusc.fr:8104) created by Marie-Paule Lefranc, Universite Montpellier II, CNRS, France.
Rakesh Anand - One of the best experts on this subject based on the ideXlab platform.
-
structure and physical map of 64 variable segments in the 3 0 8 megabase region of the Human Immunoglobulin heavy chain locus
Nature Genetics, 1993Co-Authors: Fumihiko Matsuda, Euy Kyun Shin, Hitoshi Nagaoka, Ryusuke Matsumura, Makoto Haino, Yosho Fukita, Shigeo Takaishi, Takashi Imai, John H Riley, Rakesh AnandAbstract:Structure and physical map of 64 variable segments in the 3′ 0.8–megabase region of the Human Immunoglobulin heavy–chain locus
-
structure and physical map of 64 variable segments in the 3 0 8 megabase region of the Human Immunoglobulin heavy chain locus
Nature Genetics, 1993Co-Authors: Fumihiko Matsuda, Euy Kyun Shin, Hitoshi Nagaoka, Ryusuke Matsumura, Makoto Haino, Yosho Fukita, Shigeo Takaishi, Takashi Imai, John H Riley, Rakesh AnandAbstract:We have constructed the physical map of the 0.8 megabase DNA fragment which contains the 3' 64 variable region (V) gene segments of the Human Immunoglobulin heavy chain (H) locus. The organization of the VH locus showed several features that indicate dynamic reshuffling of this locus. The sequenced 64 VH segments include 31 pseudogenes, of which 24 are highly conserved except for a few point mutations. Comparison of the 64 germline VH sequences shows that each VH family has conserved sequences, suggesting that there might be some genetic or selection mechanisms involved in maintenance of each family. The total number of the Human VH segments was estimated to be about 120, including at least 7 orphons.
Jonathon Chon Teng Chio - One of the best experts on this subject based on the ideXlab platform.
-
the effects of Human Immunoglobulin g on enhancing tissue protection and neurobehavioral recovery after traumatic cervical spinal cord injury are mediated through the neurovascular unit
Journal of Neuroinflammation, 2019Co-Authors: Jonathon Chon Teng Chio, Jian Wang, Anna Badner, James Hong, Vithushan Surendran, Michael G FehlingsAbstract:Spinal cord injury (SCI) is a condition with few effective treatment options. The blood-spinal cord barrier consists of pericytes, astrocytes, and endothelial cells, which are collectively termed the neurovascular unit. These cells support spinal cord homeostasis by expressing tight junction proteins. Physical trauma to the spinal cord disrupts the barrier, which leads to neuroinflammation by facilitating immune cell migration to the damaged site in a process involving immune cell adhesion. Immunosuppressive strategies, including methylprednisolone (MPSS), have been investigated to treat SCI. However, despite some success, MPSS has the potential to increase a patient’s susceptibility to wound infection and impaired wound healing. Hence, immunomodulation may be a more attractive approach than immunosuppression. Approved for modulating neuroinflammation in certain disorders, including Guillain-Barre syndrome, intravenous administration of Human Immunoglobulin G (hIgG) has shown promise in the setting of experimental SCI, though the optimal dose and mechanism of action remain undetermined. Female adult Wistar rats were subjected to moderate-severe clip compression injury (35 g) at the C7-T1 level and randomized to receive a single intravenous (IV) bolus of hIgG (0.02, 0.2, 0.4, 1, 2 g/kg), MPSS (0.03 g/kg), or control buffer at 15 min post-SCI. At 24 h and 6 weeks post-SCI, molecular, histological, and neurobehavioral effects of hIgG were analyzed. At 24 h post-injury, Human Immunoglobulin G co-localized with spinal cord pericytes, astrocytes, and vessels. hIgG (2 g/kg) protected the spinal cord neurovasculature after SCI by increasing tight junction protein expression and reducing inflammatory enzyme expression. Improvements in vascular integrity were associated with changes in spinal cord inflammation. Interestingly, hIgG (2 g/kg) increased serum expression of inflammatory cytokines and co-localized (without decreasing protein expression) with spinal cord vascular cell adhesion molecule-1, a protein used by immune cells to enter into inflamed tissue. Acute molecular benefits of hIgG (2 g/kg) led to greater tissue preservation, functional blood flow, and neurobehavioral recovery at 6 weeks post-SCI. Importantly, the effects of hIgG (2 g/kg) were superior to control buffer and hIgG (0.4 g/kg), and comparable with MPSS (0.03 g/kg). hIgG (2 g/kg) is a promising therapeutic approach to mitigate secondary pathology in SCI through antagonizing immune cell infiltration at the level of the neurovascular unit.