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Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
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Tandem mass spectrometry is a technique that uses multiple mass analyzers in series to obtain a higher selectivity and reduce chemical noise during analyte detection. Instruments with multiple analyzers separated by an interaction cell enable secondary fragmentation and selected study of the fragment ions.Secondary fragmentations occur in the interaction cell and can be induced by various factors. Fragmentation induced by collision with inert gases, such as N2, Ar, He, etc., is called...
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Quantification of Proteins Using Peptide Immunoaffinity Enrichment Coupled with Mass Spectrometry
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Peptide quantification by tandem mass spectrometry.

X Zhu1, D M Desiderio1,2,3

  • 1The Charles B. Stout Neuroscience Mass Spectrometry Laboratory, The University of Tennessee, Memphis, 800 Madison Avenue, Memphis, Tennessee 38163.

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Mass spectrometry (MS) and tandem mass spectrometry (MS/MS) quantify opioid peptides in human pituitary tissues. Proopiomelanocortin (POMC)-derived beta-endorphin (BE) levels were significantly altered in pituitary tumors, suggesting down-regulation.

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Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Neuroendocrinology

Background:

  • Peptide quantification in biological tissues is crucial for understanding physiological and pathological processes.
  • Mass spectrometry (MS) and tandem mass spectrometry (MS/MS) are powerful analytical techniques for peptide identification and quantification.
  • Opioid neuropeptides, such as those derived from proopiomelanocortin (POMC), play significant roles in the pituitary gland.

Purpose of the Study:

  • To review and discuss the application of MS and MS/MS for quantifying biologically important peptides in tissues.
  • To present analytical data on the measurement of specific opioid peptides, beta-endorphin (BE) and methionine enkephalin (ME), in human pituitary tissues and tumors.
  • To investigate alterations in neuropeptide systems within pituitary tumors.

Main Methods:

  • Literature review of MS and MS/MS quantification techniques for peptides.
  • Measurement of proopiomelanocortin (POMC)-derived beta-endorphin (BE) and proenkephalin-derived methionine enkephalin (ME) using MS/MS.
  • Utilized stable isotope-incorporated synthetic peptide internal standards for accurate quantification.
  • Compared peptide levels in control pituitary tissues versus pituitary tumors (PRL-secreting and non-secreting).

Main Results:

  • Established the utility of MS/MS for linking peptide molecular ions to sequence-determining fragment ions.
  • Quantified BE and ME in human pituitary tissues and tumors.
  • Observed a significant alteration in BE levels between control and tumor tissues.
  • Demonstrated a potential down-regulation of the POMC neuropeptidergic system in pituitary tumors.

Conclusions:

  • MS/MS is a reliable method for the quantification of peptides in complex biological matrices like pituitary tissue.
  • Alterations in BE levels in pituitary tumors indicate dysregulation of the POMC system.
  • These findings contribute to the understanding of neuropeptide involvement in pituitary tumor pathophysiology.