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We are analyzing https://link.springer.com/article/10.1007/bf00241259.

Title:
DNA sequences specific for Caucasian G3m(b) and (g) allotypes: allotyping at the genomic level | Immunogenetics
Description:
Assignment of the G3m(g) and (b) correlative amino acid residues was performed at the genomic level by direct sequencing of DNA from nine Caucasian individuals. Two oligonucleotide primers were used for subclass-specific enzymatic amplification of a DNA segment comprising a major portion of the second and third constant region domains (CH2 and CH3) fo the human IgG3 heavy chain gene. Comparison of the sequences of amplified DNA from individuals serologically typed as homozygous for G3m(b) or G3m(g) or as heterozygous, G3m(b,g), revealed differences in the codons for the amino acid residues 291, 296, and 384. Proline, phenylalanine, and serine at these positions corresponded to G3m(b), and leucine, tyrosine, and asparagine to G3m(g). Heterozygotic individuals, typed G3m(b,g), displayed both the G3m(b) and G3m(g) codons at these three positions. The polymorphism at each of these three codons could be identified either as the appearance, or the loss, of recognition sites for the two restriction endonucleases, Nsp BII and Rsa I. This allowed the development of a polymerase chain reaction (PCR)-based assay permitting the distinction of G3m b and G3m g alleles by analyzing the electrophoretical mobility of the DNA fragments generated by digestion of the PCR-products with Nsp BII and Rsa I.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

  • Education
  • Non-Profit & Charity
  • Science

Content Management System {📝}

What CMS is link.springer.com built with?

Custom-built

No common CMS systems were detected on Link.springer.com, and no known web development framework was identified.

Traffic Estimate {📈}

What is the average monthly size of link.springer.com audience?

🌠 Phenomenal Traffic: 5M - 10M visitors per month


Based on our best estimate, this website will receive around 7,642,828 visitors per month in the current month.

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How Does Link.springer.com Make Money? {💸}

We don't see any clear sign of profit-making.

The purpose of some websites isn't monetary gain; they're meant to inform, educate, or foster collaboration. Everyone has unique reasons for building websites. This could be an example. Link.springer.com has a secret sauce for making money, but we can't detect it yet.

Keywords {🔍}

google, scholar, grubb, human, article, dna, gmg, amino, acid, gmb, allotypes, privacy, cookies, content, genomic, level, balbín, access, genetic, markers, expl, clin, immunogenet, springer, immunoglobulin, oxford, information, publish, search, immunogenetics, sequences, specific, sequencing, chain, protein, van, ito, miyazaki, matsumoto, immunology, author, lund, analysis, data, log, journal, research, caucasian, milagros, anders,

Topics {✒️}

month download article/chapter subclass-specific enzymatic amplification constant region domains amino acid sequence article balbín dna sequences specific anders grubb polymerase chain reaction genetic markers privacy choices/manage cookies article immunogenetics aims full article pdf subclass specific amplification allele specific probes dna segment comprising dna fragments generated human immunoglobulin genes direct sequencing related subjects human immunoglobulin allotypes area de bioquímica early rheumatoid artritis european economic area check access blackwell scientific publications instant access conditions privacy policy universidad de oviedo proline phenylalanine leucine based assay permitting accepting optional cookies individuals serologically typed monoclonal anti-gm structural studies de lange journal finder publish allotypic marker gm allotypic markers lund university hospital article log oxford university press amplified dna press grubb human immunoglobulins article cite pcr-products privacy policy personal data

Schema {🗺️}

WebPage:
      mainEntity:
         headline:DNA sequences specific for Caucasian G3m(b) and (g) allotypes: allotyping at the genomic level
         description:Assignment of the G3m(g) and (b) correlative amino acid residues was performed at the genomic level by direct sequencing of DNA from nine Caucasian individuals. Two oligonucleotide primers were used for subclass-specific enzymatic amplification of a DNA segment comprising a major portion of the second and third constant region domains (CH2 and CH3) fo the human IgG3 heavy chain gene. Comparison of the sequences of amplified DNA from individuals serologically typed as homozygous for G3m(b) or G3m(g) or as heterozygous, G3m(b,g), revealed differences in the codons for the amino acid residues 291, 296, and 384. Proline, phenylalanine, and serine at these positions corresponded to G3m(b), and leucine, tyrosine, and asparagine to G3m(g). Heterozygotic individuals, typed G3m(b,g), displayed both the G3m(b) and G3m(g) codons at these three positions. The polymorphism at each of these three codons could be identified either as the appearance, or the loss, of recognition sites for the two restriction endonucleases, Nsp BII and Rsa I. This allowed the development of a polymerase chain reaction (PCR)-based assay permitting the distinction of G3m b and G3m g alleles by analyzing the electrophoretical mobility of the DNA fragments generated by digestion of the PCR-products with Nsp BII and Rsa I.
         datePublished:
         dateModified:
         pageStart:187
         pageEnd:193
         sameAs:https://doi.org/10.1007/BF00241259
         keywords:
            Codon
            Proline
            Amino Acid Residue
            Leucine
            Phenylalanine
            Immunology
            Human Genetics
            Gene Function
            Cell Biology
            Allergology
         image:
         isPartOf:
            name:Immunogenetics
            issn:
               1432-1211
               0093-7711
            volumeNumber:39
            type:
               Periodical
               PublicationVolume
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            name:Springer-Verlag
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      headline:DNA sequences specific for Caucasian G3m(b) and (g) allotypes: allotyping at the genomic level
      description:Assignment of the G3m(g) and (b) correlative amino acid residues was performed at the genomic level by direct sequencing of DNA from nine Caucasian individuals. Two oligonucleotide primers were used for subclass-specific enzymatic amplification of a DNA segment comprising a major portion of the second and third constant region domains (CH2 and CH3) fo the human IgG3 heavy chain gene. Comparison of the sequences of amplified DNA from individuals serologically typed as homozygous for G3m(b) or G3m(g) or as heterozygous, G3m(b,g), revealed differences in the codons for the amino acid residues 291, 296, and 384. Proline, phenylalanine, and serine at these positions corresponded to G3m(b), and leucine, tyrosine, and asparagine to G3m(g). Heterozygotic individuals, typed G3m(b,g), displayed both the G3m(b) and G3m(g) codons at these three positions. The polymorphism at each of these three codons could be identified either as the appearance, or the loss, of recognition sites for the two restriction endonucleases, Nsp BII and Rsa I. This allowed the development of a polymerase chain reaction (PCR)-based assay permitting the distinction of G3m b and G3m g alleles by analyzing the electrophoretical mobility of the DNA fragments generated by digestion of the PCR-products with Nsp BII and Rsa I.
      datePublished:
      dateModified:
      pageStart:187
      pageEnd:193
      sameAs:https://doi.org/10.1007/BF00241259
      keywords:
         Codon
         Proline
         Amino Acid Residue
         Leucine
         Phenylalanine
         Immunology
         Human Genetics
         Gene Function
         Cell Biology
         Allergology
      image:
      isPartOf:
         name:Immunogenetics
         issn:
            1432-1211
            0093-7711
         volumeNumber:39
         type:
            Periodical
            PublicationVolume
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         name:Springer-Verlag
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            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Milagros Balbín
            affiliation:
                  name:Lund University Hospital
                  address:
                     name:Department of Clinical Chemistry, Lund University Hospital, Lund, Sweden
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Anders Grubb
            affiliation:
                  name:Lund University Hospital
                  address:
                     name:Department of Clinical Chemistry, Lund University Hospital, Lund, Sweden
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Gerda G. de Lange
            affiliation:
                  name:Central Laboratory of the Netherlands Red Cross Blood Transfusion Service
                  address:
                     name:Central Laboratory of the Netherlands Red Cross Blood Transfusion Service, Amsterdam, Holland
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Rune Grubb
            affiliation:
                  name:University of Lund
                  address:
                     name:Department of Medical Microbiology, University of Lund, Lund, Sweden
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         name:Department of Clinical Chemistry, Lund University Hospital, Lund, Sweden
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         name:Department of Clinical Chemistry, Lund University Hospital, Lund, Sweden
         type:PostalAddress
      name:Central Laboratory of the Netherlands Red Cross Blood Transfusion Service
      address:
         name:Central Laboratory of the Netherlands Red Cross Blood Transfusion Service, Amsterdam, Holland
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               name:Department of Clinical Chemistry, Lund University Hospital, Lund, Sweden
               type:PostalAddress
            type:Organization
      name:Anders Grubb
      affiliation:
            name:Lund University Hospital
            address:
               name:Department of Clinical Chemistry, Lund University Hospital, Lund, Sweden
               type:PostalAddress
            type:Organization
      name:Gerda G. de Lange
      affiliation:
            name:Central Laboratory of the Netherlands Red Cross Blood Transfusion Service
            address:
               name:Central Laboratory of the Netherlands Red Cross Blood Transfusion Service, Amsterdam, Holland
               type:PostalAddress
            type:Organization
      name:Rune Grubb
      affiliation:
            name:University of Lund
            address:
               name:Department of Medical Microbiology, University of Lund, Lund, Sweden
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Department of Clinical Chemistry, Lund University Hospital, Lund, Sweden
      name:Department of Clinical Chemistry, Lund University Hospital, Lund, Sweden
      name:Central Laboratory of the Netherlands Red Cross Blood Transfusion Service, Amsterdam, Holland
      name:Department of Medical Microbiology, University of Lund, Lund, Sweden
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