We are analyzing https://link.springer.com/article/10.1007/bf02115689.

Title:
The mouse muscle creatine kinase cDNA and deduced amino acid sequences: Comparison to evolutionarily related enzymes | Journal of Molecular Evolution
Description:
The nucleotide sequence of cloned DNA corresponding to full-length mouse muscle creatine kinase mRNA has been determined. This 1415 base pair DNA sequence and the deduced 381 amino acid sequence of the protein have been compared to creatine kinase sequences from other vertebrate species and to invertebrate guanidino kinase sequences. These comparisons show that the vertebrate muscle creatine kinases constitute a remarkably conserved protein family with a unit evolutionary period of 30. The creatine kinases also retain marked sequence similarity with the more distantly related invertebrate guanidino kinases. A portion of the sequence, presumably part of the ATP binding site, shows similarity to other nucleotide binding proteins with diverse functions. Comparisons of the untranslated regions of the creatine kinase cDNA sequences show that the 5′ untranslated regions are more highly conserved than are the 3′ untranslated regions; this may point to some regulatory function in the 5′ region.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

Education
Science
Health & Fitness

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 5,000,019 visitors per month in the current month.
However, some sources were not loaded, we suggest to reload the page to get complete results.

check SE Ranking
check Ahrefs
check Similarweb
check Ubersuggest
check Semrush

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

We find it hard to spot revenue streams.

Earning money isn't the goal of every website; some are designed to offer support or promote social causes. People have different reasons for creating websites. This might be one such reason. Link.springer.com could be getting rich in stealth mode, or the way it's monetizing isn't detectable.

Keywords {🔍}

google, scholar, pubmed, kinase, creatine, sequence, muscle, protein, article, cdna, biol, sequences, amino, biochem, acid, human, usa, nucleotide, kinases, cell, proc, nature, privacy, cookies, site, content, journal, molecular, evolution, related, chamberlain, dna, access, chem, natl, acad, sci, res, analysis, publish, research, search, mouse, enzymes, jaynes, mrna, guanidino, skeletal, mol, eppenberger,

Topics {✒️}

month download article/chapter muscle-specific creatine kinase acetylcholine receptor-enriched membranes camp-dependent protein kinase predicted nucleotide-binding properties lobster-muscle arginine kinase hormone-activated transmembrane signalling double-digest restriction fragments invertebrate guanidino kinases dideoxy chain-termination method full-length cdna human heart muscle porcine skeletal muscle chicken skeletal muscle creatine kinases mm amino acid sequence complete nucleotide sequence molecular evolution aims creatine kinase sequences full article pdf differentiating mouse myoblasts mitochondrial creatine kinase creatine kinase induction creatine kinase isozymes mm creatine kinase creatine kinase isoenzymes nucleotide binding proteins related subjects cdna clones coding adenosine 5′-triphosphatecreatine phosphotransferase privacy choices/manage cookies homarus vulgaris muscle lumbricus terrestris muscle atp binding site evolutionarily related enzymes protein sequencing estronen-induced protein chimeric protein homologous separate protein families cold spring harbor creatine kinases tissue-specific isozymes chain-terminating inhibitors coding region sequences nucleotide sequence european economic area scope submit manuscript unit evolutionary period check access thiol group reactivity

Schema {🗺️}

WebPage:
      mainEntity:
         headline:The mouse muscle creatine kinase cDNA and deduced amino acid sequences: Comparison to evolutionarily related enzymes
         description:The nucleotide sequence of cloned DNA corresponding to full-length mouse muscle creatine kinase mRNA has been determined. This 1415 base pair DNA sequence and the deduced 381 amino acid sequence of the protein have been compared to creatine kinase sequences from other vertebrate species and to invertebrate guanidino kinase sequences. These comparisons show that the vertebrate muscle creatine kinases constitute a remarkably conserved protein family with a unit evolutionary period of 30. The creatine kinases also retain marked sequence similarity with the more distantly related invertebrate guanidino kinases. A portion of the sequence, presumably part of the ATP binding site, shows similarity to other nucleotide binding proteins with diverse functions. Comparisons of the untranslated regions of the creatine kinase cDNA sequences show that the 5′ untranslated regions are more highly conserved than are the 3′ untranslated regions; this may point to some regulatory function in the 5′ region.
         datePublished:
         dateModified:
         pageStart:334
         pageEnd:341
         sameAs:https://doi.org/10.1007/BF02115689
         keywords:
            Creatine kinase
            cDNA
            Muscle
            Guanidino kinase
            Nucleotide binding
            Kinase
            Evolutionary Biology
            Microbiology
            Plant Sciences
            Plant Genetics and Genomics
            Animal Genetics and Genomics
            Cell Biology
         image:
         isPartOf:
            name:Journal of Molecular Evolution
            issn:
               1432-1432
               0022-2844
            volumeNumber:22
            type:
               Periodical
               PublicationVolume
         publisher:
            name:Springer-Verlag
            logo:
               url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
               type:ImageObject
            type:Organization
         author:
               name:J. N. Buskin
               affiliation:
                     name:University of Washington
                     address:
                        name:Department of Biochemistry, University of Washington, Seattle, USA
                        type:PostalAddress
                     type:Organization
               type:Person
               name:J. B. Jaynes
               affiliation:
                     name:University of Washington
                     address:
                        name:Department of Biochemistry, University of Washington, Seattle, USA
                        type:PostalAddress
                     type:Organization
               type:Person
               name:J. S. Chamberlain
               affiliation:
                     name:University of Washington
                     address:
                        name:Department of Biochemistry, University of Washington, Seattle, USA
                        type:PostalAddress
                     type:Organization
               type:Person
               name:S. D. Hauschka
               affiliation:
                     name:University of Washington
                     address:
                        name:Department of Biochemistry, University of Washington, Seattle, USA
                        type:PostalAddress
                     type:Organization
               type:Person
         isAccessibleForFree:
         hasPart:
            isAccessibleForFree:
            cssSelector:.main-content
            type:WebPageElement
         type:ScholarlyArticle
      context:https://schema.org
ScholarlyArticle:
      headline:The mouse muscle creatine kinase cDNA and deduced amino acid sequences: Comparison to evolutionarily related enzymes
      description:The nucleotide sequence of cloned DNA corresponding to full-length mouse muscle creatine kinase mRNA has been determined. This 1415 base pair DNA sequence and the deduced 381 amino acid sequence of the protein have been compared to creatine kinase sequences from other vertebrate species and to invertebrate guanidino kinase sequences. These comparisons show that the vertebrate muscle creatine kinases constitute a remarkably conserved protein family with a unit evolutionary period of 30. The creatine kinases also retain marked sequence similarity with the more distantly related invertebrate guanidino kinases. A portion of the sequence, presumably part of the ATP binding site, shows similarity to other nucleotide binding proteins with diverse functions. Comparisons of the untranslated regions of the creatine kinase cDNA sequences show that the 5′ untranslated regions are more highly conserved than are the 3′ untranslated regions; this may point to some regulatory function in the 5′ region.
      datePublished:
      dateModified:
      pageStart:334
      pageEnd:341
      sameAs:https://doi.org/10.1007/BF02115689
      keywords:
         Creatine kinase
         cDNA
         Muscle
         Guanidino kinase
         Nucleotide binding
         Kinase
         Evolutionary Biology
         Microbiology
         Plant Sciences
         Plant Genetics and Genomics
         Animal Genetics and Genomics
         Cell Biology
      image:
      isPartOf:
         name:Journal of Molecular Evolution
         issn:
            1432-1432
            0022-2844
         volumeNumber:22
         type:
            Periodical
            PublicationVolume
      publisher:
         name:Springer-Verlag
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:J. N. Buskin
            affiliation:
                  name:University of Washington
                  address:
                     name:Department of Biochemistry, University of Washington, Seattle, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:J. B. Jaynes
            affiliation:
                  name:University of Washington
                  address:
                     name:Department of Biochemistry, University of Washington, Seattle, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:J. S. Chamberlain
            affiliation:
                  name:University of Washington
                  address:
                     name:Department of Biochemistry, University of Washington, Seattle, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:S. D. Hauschka
            affiliation:
                  name:University of Washington
                  address:
                     name:Department of Biochemistry, University of Washington, Seattle, USA
                     type:PostalAddress
                  type:Organization
            type:Person
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
["Periodical","PublicationVolume"]:
      name:Journal of Molecular Evolution
      issn:
         1432-1432
         0022-2844
      volumeNumber:22
Organization:
      name:Springer-Verlag
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:University of Washington
      address:
         name:Department of Biochemistry, University of Washington, Seattle, USA
         type:PostalAddress
      name:University of Washington
      address:
         name:Department of Biochemistry, University of Washington, Seattle, USA
         type:PostalAddress
      name:University of Washington
      address:
         name:Department of Biochemistry, University of Washington, Seattle, USA
         type:PostalAddress
      name:University of Washington
      address:
         name:Department of Biochemistry, University of Washington, Seattle, USA
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:J. N. Buskin
      affiliation:
            name:University of Washington
            address:
               name:Department of Biochemistry, University of Washington, Seattle, USA
               type:PostalAddress
            type:Organization
      name:J. B. Jaynes
      affiliation:
            name:University of Washington
            address:
               name:Department of Biochemistry, University of Washington, Seattle, USA
               type:PostalAddress
            type:Organization
      name:J. S. Chamberlain
      affiliation:
            name:University of Washington
            address:
               name:Department of Biochemistry, University of Washington, Seattle, USA
               type:PostalAddress
            type:Organization
      name:S. D. Hauschka
      affiliation:
            name:University of Washington
            address:
               name:Department of Biochemistry, University of Washington, Seattle, USA
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Department of Biochemistry, University of Washington, Seattle, USA
      name:Department of Biochemistry, University of Washington, Seattle, USA
      name:Department of Biochemistry, University of Washington, Seattle, USA
      name:Department of Biochemistry, University of Washington, Seattle, USA
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

External Links {🔗}(112)

Analytics and Tracking {📊}

Google Tag Manager

Libraries {📚}

Clipboard.js
Prism.js

CDN Services {📦}

Crossref

3.94s.

LINK . SPRINGER . COM {}