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Study · Not a test of the peptide alone · 1994

5 results

Peptide synthesis catalyzed by the Glu/Asp-specific endopeptidase. Influence of the ester leaving group of the acyl donor on yield and catalytic efficiency.

Bongers J, Liu W, Lambros T, Breddam K, Campbell RM, Felix AM, Heimer EP

International journal of peptide and protein research1 Aug 1994Cited by 3 (Europe PMC)

PMID7982755 (opens in a new tab)DOI10.1111/j.1399-3011.1994.tb00566.x (opens in a new tab)PepBankPUB-07982755
Publisher pagePubMedAsk about this study
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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 study5

No result from this study comes from a test of the peptide.

Studies that did not test the peptide alone5

In this study, Sermorelin was a lab tool or a carrier, part of a mix, or the subject of a lab method. These results are not evidence about taking Sermorelin.

  1. 01LabNot a test of Sermorelin aloneIn vitro (cell-free)Other

    Glu/Asp-specific endopeptidase (GSE) from Bacillus licheniformis was an efficient catalyst for the segment condensation that gives a GRF(1-29)-NH2 analog.

    In plain wordsIn lab chemistry, an enzyme from bacteria worked well to join peptide pieces into a GRF analog.

    Peptide
    Sermorelin
    Outcome
    Not applicableGSE as catalyst for segment condensation
    Study

    n: not reported in source

    enzymatic semisynthesis
    Outcome group
    Synthesis and manufacturing · Pharmacology

    Source sentences

    Summary
    In this paper we report on the use of the recently isolated Glu/Asp-specific endopeptidase (GSE) from Bacillus licheniformis, which is shown to be an efficient catalyst for the segment condensation of 2 and 3.

    In this study, Sermorelin was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Sermorelin.

  2. 02LabNot a test of Sermorelin aloneIn vitro (cell-free)Other

    GSE was more stable than V8 protease under the conditions used.

    In plain wordsIn lab chemistry, GSE was more stable than V8 protease under the same conditions.

    Peptide
    Sermorelin
    Outcome
    Not applicableStability of GSE versus V8 protease
    Study

    n: not reported in source

    enzymatic semisynthesis
    Outcome group
    Synthesis and manufacturing · Pharmacology

    Source sentences

    Summary
    GSE is more stable than the V8 protease under the conditions employed (20% DMF, pH 8.2, 37 degrees C).

    In this study, Sermorelin was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Sermorelin.

  3. 03LabNot a test of Sermorelin aloneIn vitro (cell-free)Other

    Conversion of segment 2 into analog 4 was limited by proteolysis at Asp3-Ala4 and Asp25-Ile26.

    In plain wordsIn lab chemistry, unwanted cutting of the peptide at two sites limited how much product formed.

    Peptide
    Sermorelin
    Outcome
    Not applicableProteolysis limiting conversion
    Study

    n: not reported in source

    enzymatic semisynthesis
    Outcome group
    Synthesis and manufacturing · Pharmacology

    Source sentences

    Summary
    The extent of conversion of 2 into 4 is limited by proteolyses at Asp3-Ala4 and Asp25-Ile26.

    In this study, Sermorelin was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Sermorelin.

  4. 04LabNot a test of Sermorelin aloneIn vitro (cell-free)Other

    Proteolysis was virtually eliminated by use of the appropriate ester leaving group.

    In plain wordsIn lab chemistry, choosing the right ester group almost stopped the unwanted cutting.

    Peptide
    Sermorelin
    Outcome
    Not applicableEffect of ester leaving group on proteolysis
    Study

    n: not reported in source

    enzymatic semisynthesis
    Outcome group
    Synthesis and manufacturing · Pharmacology

    Source sentences

    Summary
    However, this proteolysis is virtually eliminated by use of the appropriate ester leaving group, R.

    In this study, Sermorelin was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Sermorelin.

  5. 05LabNot a test of Sermorelin aloneIn vitro (cell-free)Other

    Conversion of segment 2 into analog 4 increased with increasing GSE specificity (Vmax/Km) for the tripeptide ester.

    In plain wordsIn lab chemistry, more product formed when the enzyme was more specific for the tripeptide ester used.

    Peptide
    Sermorelin
    Outcome
    Not applicableKinetics of GSE-catalyzed condensation
    Study

    n: not reported in source

    enzymatic semisynthesis
    Outcome group
    Synthesis and manufacturing · Pharmacology

    Source sentences

    Summary
    revealed that rate of aminolysis versus proteolysis, and hence the conversion of 2 into 4, increase with increasing specificity (Vmax/Km) of GSE for the tripeptide ester

    In this study, Sermorelin was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Sermorelin.

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

    10 Oct 2026, 10:21 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.

Publication types

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