We are analyzing https://link.springer.com/article/10.1007/s12033-007-0048-7.

Title:
Alterations in Antioxidant Enzymes During Aging in Humans | Molecular Biotechnology
Description:
The oxidative stress theory of aging offers the best mechanistic elucidation of the aging phenomenon and other age-related diseases. The susceptibility of an individual depends on the antioxidant status of the body. In humans, the antioxidant system includes a number of antioxidant enzymes such as superoxide dismutase (SOD) and catalase (CAT), nonenzymatic antioxidants such as glutathione (GSH), protein –SH, ascorbic acid, and uric acid, and dietary antioxidants. Antioxidant enzymes form the first line of defense against reactive oxygen species. In an earlier report, we showed that the plasma antioxidant potential in humans decreases as a function of age and that there are compensatory mechanisms operating in the body which are induced to maintain the antioxidant capacity during aging. In the present study, we report the relationship between human aging and antioxidant enzymes SOD and CAT; we also correlate the activity of these enzymes with the antioxidant capacity of the plasma. Our results show a significantly higher plasma SOD and CAT activity in older individuals than in younger individuals. The induction in activity of SOD and CAT during human aging may be a compensatory response of the individual to an increased oxidative stress.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

Science
Education
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 7,626,432 visitors per month in the current month.

check SE Ranking
check Ahrefs
check Similarweb
check Ubersuggest
check Semrush

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

We can't see how the site brings in money.

Not all websites focus on profit; some are designed to educate, connect people, or share useful tools. People create websites for numerous reasons. And this could be one such example. Link.springer.com could be getting rich in stealth mode, or the way it's monetizing isn't detectable.

Keywords {🔍}

google, scholar, article, antioxidant, aging, cas, oxidative, pubmed, enzymes, stress, journal, research, human, free, radical, rizvi, superoxide, catalase, plasma, privacy, cookies, content, dismutase, activity, access, biology, function, publish, search, alterations, humans, maurya, theory, sod, cat, chemistry, activities, medicine, data, information, log, august, syed, ibrahim, agerelated, antioxidants, age, capacity, chapter, rat,

Topics {✒️}

syed ibrahim rizvi month download article/chapter oxidative stress-related damage full article pdf privacy choices/manage cookies malondialdehyde levels related free radical research age-related alterations antioxidant system includes erythrocyte antioxidant enzymes article rizvi age-related diseases superoxide anion radical increased oxidative stress oxidative stress parameters reactive oxygen species clinica chimica acta controlled diets high mouse skeletal muscles folin phenol reagent cardiac interfibriller mitochondria antioxidative enzyme activities conditions privacy policy oxidative stress theory related subjects oxidative stress markers therapeutic antioxidant interventions antioxidant enzymes form european economic area healthy women depends mitochondrial dna mutation antioxidant enzyme activities free radical biology plasma antioxidant potential accepting optional cookies free radical theory university grants commission antioxidant enzymes sod author information authors main content log check access instant access compensatory mechanisms operating superoxide dismutase york academy sciences journal finder publish article log human plasma catalase activities article cite

Questions {❓}

Which potential markers ?

Schema {🗺️}

WebPage:
      mainEntity:
         headline:Alterations in Antioxidant Enzymes During Aging in Humans
         description:The oxidative stress theory of aging offers the best mechanistic elucidation of the aging phenomenon and other age-related diseases. The susceptibility of an individual depends on the antioxidant status of the body. In humans, the antioxidant system includes a number of antioxidant enzymes such as superoxide dismutase (SOD) and catalase (CAT), nonenzymatic antioxidants such as glutathione (GSH), protein –SH, ascorbic acid, and uric acid, and dietary antioxidants. Antioxidant enzymes form the first line of defense against reactive oxygen species. In an earlier report, we showed that the plasma antioxidant potential in humans decreases as a function of age and that there are compensatory mechanisms operating in the body which are induced to maintain the antioxidant capacity during aging. In the present study, we report the relationship between human aging and antioxidant enzymes SOD and CAT; we also correlate the activity of these enzymes with the antioxidant capacity of the plasma. Our results show a significantly higher plasma SOD and CAT activity in older individuals than in younger individuals. The induction in activity of SOD and CAT during human aging may be a compensatory response of the individual to an increased oxidative stress.
         datePublished:2007-08-01T00:00:00Z
         dateModified:2007-08-01T00:00:00Z
         pageStart:58
         pageEnd:61
         sameAs:https://doi.org/10.1007/s12033-007-0048-7
         keywords:
            Human aging
            Oxidative stress
            Superoxide dismutase
            Catalase
            Biotechnology
            Biochemistry
            general
            Cell Biology
            Protein Science
            Biological Techniques
            Human Genetics
         image:
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs12033-007-0048-7/MediaObjects/12033_2007_48_Fig1_HTML.gif
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs12033-007-0048-7/MediaObjects/12033_2007_48_Fig2_HTML.gif
         isPartOf:
            name:Molecular Biotechnology
            issn:
               1559-0305
               1073-6085
            volumeNumber:37
            type:
               Periodical
               PublicationVolume
         publisher:
            name:Humana Press Inc
            logo:
               url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
               type:ImageObject
            type:Organization
         author:
               name:Syed Ibrahim Rizvi
               affiliation:
                     name:University of Allahabad
                     address:
                        name:Department of Biochemistry, University of Allahabad, Allahabad, India
                        type:PostalAddress
                     type:Organization
               email:[email protected]
               type:Person
               name:Pawan Kumar Maurya
               affiliation:
                     name:University of Allahabad
                     address:
                        name:Department of Biochemistry, University of Allahabad, Allahabad, India
                        type:PostalAddress
                     type:Organization
               type:Person
         isAccessibleForFree:
         hasPart:
            isAccessibleForFree:
            cssSelector:.main-content
            type:WebPageElement
         type:ScholarlyArticle
      context:https://schema.org
ScholarlyArticle:
      headline:Alterations in Antioxidant Enzymes During Aging in Humans
      description:The oxidative stress theory of aging offers the best mechanistic elucidation of the aging phenomenon and other age-related diseases. The susceptibility of an individual depends on the antioxidant status of the body. In humans, the antioxidant system includes a number of antioxidant enzymes such as superoxide dismutase (SOD) and catalase (CAT), nonenzymatic antioxidants such as glutathione (GSH), protein –SH, ascorbic acid, and uric acid, and dietary antioxidants. Antioxidant enzymes form the first line of defense against reactive oxygen species. In an earlier report, we showed that the plasma antioxidant potential in humans decreases as a function of age and that there are compensatory mechanisms operating in the body which are induced to maintain the antioxidant capacity during aging. In the present study, we report the relationship between human aging and antioxidant enzymes SOD and CAT; we also correlate the activity of these enzymes with the antioxidant capacity of the plasma. Our results show a significantly higher plasma SOD and CAT activity in older individuals than in younger individuals. The induction in activity of SOD and CAT during human aging may be a compensatory response of the individual to an increased oxidative stress.
      datePublished:2007-08-01T00:00:00Z
      dateModified:2007-08-01T00:00:00Z
      pageStart:58
      pageEnd:61
      sameAs:https://doi.org/10.1007/s12033-007-0048-7
      keywords:
         Human aging
         Oxidative stress
         Superoxide dismutase
         Catalase
         Biotechnology
         Biochemistry
         general
         Cell Biology
         Protein Science
         Biological Techniques
         Human Genetics
      image:
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs12033-007-0048-7/MediaObjects/12033_2007_48_Fig1_HTML.gif
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs12033-007-0048-7/MediaObjects/12033_2007_48_Fig2_HTML.gif
      isPartOf:
         name:Molecular Biotechnology
         issn:
            1559-0305
            1073-6085
         volumeNumber:37
         type:
            Periodical
            PublicationVolume
      publisher:
         name:Humana Press Inc
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Syed Ibrahim Rizvi
            affiliation:
                  name:University of Allahabad
                  address:
                     name:Department of Biochemistry, University of Allahabad, Allahabad, India
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
            name:Pawan Kumar Maurya
            affiliation:
                  name:University of Allahabad
                  address:
                     name:Department of Biochemistry, University of Allahabad, Allahabad, India
                     type:PostalAddress
                  type:Organization
            type:Person
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
["Periodical","PublicationVolume"]:
      name:Molecular Biotechnology
      issn:
         1559-0305
         1073-6085
      volumeNumber:37
Organization:
      name:Humana Press Inc
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:University of Allahabad
      address:
         name:Department of Biochemistry, University of Allahabad, Allahabad, India
         type:PostalAddress
      name:University of Allahabad
      address:
         name:Department of Biochemistry, University of Allahabad, Allahabad, India
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Syed Ibrahim Rizvi
      affiliation:
            name:University of Allahabad
            address:
               name:Department of Biochemistry, University of Allahabad, Allahabad, India
               type:PostalAddress
            type:Organization
      email:[email protected]
      name:Pawan Kumar Maurya
      affiliation:
            name:University of Allahabad
            address:
               name:Department of Biochemistry, University of Allahabad, Allahabad, India
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Department of Biochemistry, University of Allahabad, Allahabad, India
      name:Department of Biochemistry, University of Allahabad, Allahabad, India
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

External Links {🔗}(74)

Analytics and Tracking {📊}

Google Tag Manager

Libraries {📚}

Clipboard.js
Prism.js

CDN Services {📦}

Crossref

4.2s.

LINK . SPRINGER . COM {}