Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Automated triple assay for proline, hydroxyproline and hydroxylysine on one single sample

N Blumenkrantz

    Clinical Biochemistry
    |August 1, 1980
    PubMed
    Summary
    This summary is machine-generated.

    Related Concept Videos

    You might also read

    Related Articles

    Articles linked to this work by shared authors, journal, and citation graph.

    Sort by
    Same author

    An LC/MS/MS method for the quantitation of MTIC (5-(3-N-methyltriazen-1-yl)-imidazole-4-carboxamide), a bioconversion product of temozolomide, in rat and dog plasma.

    Journal of pharmaceutical and biomedical analysis·2000
    Same author

    In vitro metabolism of 10-(3-chlorophenyl)-6,8,9,10-tetrahydrobenzo[b][1,8]naphthyridin-5(7H)- one, a topical antipsoriatic agent. Use of precision-cut rat, dog, monkey and human liver slices, and chemical synthesis of metabolites.

    Biopharmaceutics & drug disposition·1998
    Same author

    Altered collagen in colonic polyps.

    Acta pathologica, microbiologica, et immunologica Scandinavica. Section A, Pathology·1985
    Same author

    Characterization of collagen hydroxylysyl glycosyltransferases as mainly intramembranous microsomal enzymes.

    The Journal of biological chemistry·1984
    Same author

    Characterization of an amyloid fibril protein from localized amyloidosis of the skin as lambda immunoglobulin light chains of variable subgroup I (A lambda I).

    Clinical and experimental immunology·1981
    Same author

    Three automated quantitative assays for serum proteins.

    Clinical biochemistry·1980

    New assays offer rapid, sensitive, and specific quantification of proline, hydroxyproline, and hydroxylysine. Automation and simplified manual methods improve efficiency for amino acid analysis in research.

    Area of Science:

    • Biochemistry
    • Analytical Chemistry

    Background:

    • Accurate quantification of amino acids like proline, hydroxyproline, and hydroxylysine is crucial in biochemical research.
    • Existing methods for amino acid analysis can be time-consuming and require multiple samples.

    Purpose of the Study:

    • To develop a new, rapid, sensitive, and specific assay for quantitative proline determination.
    • To present an automated procedure for simultaneous detection of proline, hydroxyproline, and hydroxylysine.
    • To introduce a simplified, rapid manual assay for hydroxylysine.

    Main Methods:

    • Quantitative determination of proline using glacial acetic acid-formaldehyde as a solvent for ninhydrin.
    • Serial automated procedure for simultaneous detection of three amino acids from a single sample.

    Related Experiment Videos

  • Development of a simplified manual assay for hydroxylysine detection.
  • Main Results:

    • The new proline assay is quick, sensitive, specific, and automatable.
    • The simultaneous triple assay is as specific, reproducible, and sensitive as individual assays, improving sample efficiency.
    • The manual hydroxylysine assay is rapid, sensitive, and specific, simplifying previous methods.

    Conclusions:

    • The developed assays enhance the efficiency and accuracy of amino acid quantification.
    • Automation and simplified procedures offer significant advantages for biochemical and analytical laboratories.
    • These methods provide valuable tools for researchers studying collagen and other proline-rich proteins.