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Study · Ex vivo tissue · pig · 1991

3 results

In vitro stability of growth hormone releasing factor (GRF) analogs in porcine plasma.

Su CM, Jensen LR, Heimer EP, Felix AM, Pan YC, Mowles TF

Hormone and metabolic research = Hormon- und Stoffwechselforschung = Hormones et metabolisme1 Jan 1991Cited by 26 (Europe PMC)

Summary

The text of this summary is not shown here, because the article license does not allow reuse. Read it at the source (opens in a new tab)

Text rights: Publisher copyright. Results still quote short attributed sentences.

Results from this study3

3 results from studies that gave the peptide. No result from this study comes from people.

  1. 01LabEx vivo tissuePharmacokinetics

    In porcine plasma in vitro, GRF(1-29)-NH2 was rapidly broken down, with a degradation half-life of 13 min.

    In plain wordsIn lab tests with pig plasma, GRF(1-29)-NH2 broke down quickly, with a half-life of about 13 minutes.

    Peptide
    Sermorelin
    Outcome
    Not applicableDegradation half-life in plasma
    Study

    pign: not reported in source

    porcine plasma
    Outcome group
    Pharmacokinetics · Pharmacology
    Studied dose
    Dose not stated

    Measurements

    half-life
    13 min
    porcine plasma, 37 degrees C

    Source sentences

    Summary
    GRF(1-29)-NH2 was rapidly broken down in the plasma with a degradation rate of t1/2 = 13 min.
    1 context sentence
    Summary · context
    GRF analogs were incubated in porcine plasma at 37 degrees C, extracted and subsequently analyzed using high performance liquid chromatography (HPLC).
  2. 02LabEx vivo tissueOther

    In porcine plasma in vitro, the primary degradation product of GRF(1-29)-NH2 was GRF(3-29)-NH2.

    In plain wordsIn lab tests with pig plasma, GRF(1-29)-NH2 was mainly cut to a shorter piece lacking the first two amino acids.

    Peptide
    Sermorelin
    Outcome
    Not applicablePrimary degradation product
    Study

    pign: not reported in source

    porcine plasma
    Outcome group
    Pharmacokinetics · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    The primary degradation product was identified as GRF(3-29)-NH2.
    1 context sentence
    Summary · context
    GRF analogs were incubated in porcine plasma at 37 degrees C, extracted and subsequently analyzed using high performance liquid chromatography (HPLC).
  3. 03LabEx vivo tissueMechanism

    In porcine plasma in vitro, cleavage between positions 2 and 3 of the peptide was not inhibited by trasylol alone but was dramatically reduced by diprotin A with trasylol.

    In plain wordsIn lab tests with pig plasma, the first cut was blocked by diprotin A plus trasylol together, but not by trasylol alone.

    Peptide
    Sermorelin
    Outcome
    MixedInhibition of cleavage between positions 2 and 3
    Study

    pign: not reported in source

    porcine plasma
    Outcome group
    Pharmacokinetics · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    The cleavage between the 2 and 3 position of the peptide was not inhibited by trasylol at a concentration of 1,000 KIU/ml but was dramatically reduced by the combined use of diprotin A and trasylol.
    1 context sentence
    Summary · context
    GRF analogs were incubated in porcine plasma at 37 degrees C, extracted and subsequently analyzed using high performance liquid chromatography (HPLC).

AI wrote and checked these results. AI can make mistakes, so check important results against the source.

Version history

PepBank keeps every version of the data on this study. Status changes from Retraction Watch, Europe PMC and Crossref are listed with their source.

  1. Version 2Current

    9 Oct 2026, 19:08 UTC

    Study results updated

  2. Version 1

    9 Oct 2026, 03:13 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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