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[Leu-enkephalin homogeneously labeled with tritium in studying the Selank inhibiting effect on the enkephalin-degrading enzymes of human plasma].
Bioorg Khim. 2004 May-Jun; 30(3):234-40.BK

Abstract

A method of analysis of enkephalinase activity in blood plasma based on the application of Leu-enkephalin generally labeled with tritium at all its amino acid residues was developed. The method allows the simultaneous estimation of activity of several peptidases in microquantities of tissues. [G-3H]Leu-enkephalin was prepared by the method of solid phase catalytic isotope exchange (120 Ci/mmol) and subjected to proteolysis by the treatment with blood plasma. The resulting radioactive metabolites were separated by HPLC in the presence of the mixture of unlabeled fragments of Leu-enkephalin as internal standards. It was shown that aminopeptidases, dipeptidylaminopeptidases, and dipeptidylcarboxypeptidases respond for approximately 80%, 2%, and 10% of the total enzymatic activity, respectively. The new pathway of degradation of Leu-enkephalin by carboxypeptidase that provides for approximately 6% of the total enkephalin-degrading activity was discovered. Bestatin was shown to predominantly inhibit aminopeptidases and carboxypeptidases, whereas Selank is more specific for carboxypeptidases and dicarboxypeptidases. The English version of the paper: Russian Journal of Bioorganic Chemistry, 2004, vol. 30, no. 3; see also http://www.maik.ru.

Authors

No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

rus

PubMed ID

15344652

Citation

Zolotarev, Iu A., et al. "[Leu-enkephalin Homogeneously Labeled With Tritium in Studying the Selank Inhibiting Effect On the Enkephalin-degrading Enzymes of Human Plasma]." Bioorganicheskaia Khimiia, vol. 30, no. 3, 2004, pp. 234-40.
Zolotarev IuA, Sokolov OIu, Kost NV, et al. [Leu-enkephalin homogeneously labeled with tritium in studying the Selank inhibiting effect on the enkephalin-degrading enzymes of human plasma]. Bioorg Khim. 2004;30(3):234-40.
Zolotarev, I. u. A., Sokolov, O. I. u., Kost, N. V., Vas'kovskiĭ, B. V., Miasoedov, N. F., & Zozulia, A. A. (2004). [Leu-enkephalin homogeneously labeled with tritium in studying the Selank inhibiting effect on the enkephalin-degrading enzymes of human plasma]. Bioorganicheskaia Khimiia, 30(3), 234-40.
Zolotarev IuA, et al. [Leu-enkephalin Homogeneously Labeled With Tritium in Studying the Selank Inhibiting Effect On the Enkephalin-degrading Enzymes of Human Plasma]. Bioorg Khim. 2004 May-Jun;30(3):234-40. PubMed PMID: 15344652.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - [Leu-enkephalin homogeneously labeled with tritium in studying the Selank inhibiting effect on the enkephalin-degrading enzymes of human plasma]. AU - Zolotarev,Iu A, AU - Sokolov,O Iu, AU - Kost,N V, AU - Vas'kovskiĭ,B V, AU - Miasoedov,N F, AU - Zozulia,A A, PY - 2004/9/4/pubmed PY - 2005/2/24/medline PY - 2004/9/4/entrez SP - 234 EP - 40 JF - Bioorganicheskaia khimiia JO - Bioorg Khim VL - 30 IS - 3 N2 - A method of analysis of enkephalinase activity in blood plasma based on the application of Leu-enkephalin generally labeled with tritium at all its amino acid residues was developed. The method allows the simultaneous estimation of activity of several peptidases in microquantities of tissues. [G-3H]Leu-enkephalin was prepared by the method of solid phase catalytic isotope exchange (120 Ci/mmol) and subjected to proteolysis by the treatment with blood plasma. The resulting radioactive metabolites were separated by HPLC in the presence of the mixture of unlabeled fragments of Leu-enkephalin as internal standards. It was shown that aminopeptidases, dipeptidylaminopeptidases, and dipeptidylcarboxypeptidases respond for approximately 80%, 2%, and 10% of the total enzymatic activity, respectively. The new pathway of degradation of Leu-enkephalin by carboxypeptidase that provides for approximately 6% of the total enkephalin-degrading activity was discovered. Bestatin was shown to predominantly inhibit aminopeptidases and carboxypeptidases, whereas Selank is more specific for carboxypeptidases and dicarboxypeptidases. The English version of the paper: Russian Journal of Bioorganic Chemistry, 2004, vol. 30, no. 3; see also http://www.maik.ru. SN - 0132-3423 UR - https://www.unboundmedicine.com/medline/citation/15344652/[Leu_enkephalin_homogeneously_labeled_with_tritium_in_studying_the_Selank_inhibiting_effect_on_the_enkephalin_degrading_enzymes_of_human_plasma]_ DB - PRIME DP - Unbound Medicine ER -