| Brain endo-oligopeptidase B: inactivation of LH-RH by hydrolysis of the Pro9-Gly-NH2(10) peptide bond. | |
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MedLine Citation:
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PMID: 6763542 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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1. The site of hydrolysis of rabbit brain endo-oligopeptidase B acting on luteinizing hormone-releasing hormone (LH-RH) was determined by isolating the products by chromatography on Aminex A-5 resin developed with pyridine-acetic acid buffer. The products [des-Gly-NH2(10)]-LH-RH, glycinamide and unhydrolyzed LH-RH were identified and shown to be homogeneous by amino acid analysis and high-voltage paper electrophoresis at pH 2.1 and 3.5 and recovered in yields of 58, 65 and 23%, respectively. 2. A sensitive analytical method for the measurement of 4-40 nmoles of glycinamide with an automatic amino acid analyzer was described. Aminex A-5 resin (0.90 x 15 cm) was eluted with sodium citrate buffer, pH 3.25 (0.2 N Na+) at 32 degrees C and ninhydrin was used for detection. 3. The data show that endo-oligopeptidase B acts as a post-proline cleaving enzyme that inactivates LH-RH by hydrolysis of the Pro9-Gly-NH2(10) peptide bond. The enzyme may participate in the metabolism of LH-RH in the central nervous system. |
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Authors:
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A C Camargo; A C Spadaro; A R Martins; L J Greene |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Brazilian journal of medical and biological research = Revista brasileira de pesquisas médicas e biológicas / Sociedade Brasileira de Biofísica ... [et al.] Volume: 15 ISSN: 0100-879X ISO Abbreviation: Braz. J. Med. Biol. Res. Publication Date: 1982 Oct |
Date Detail:
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Created Date: 1983-07-08 Completed Date: 1983-07-08 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 8112917 Medline TA: Braz J Med Biol Res Country: BRAZIL |
Other Details:
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Languages: eng Pagination: 239-45 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Brain / enzymology* Chromatography Cysteine Endopeptidases* Electrophoresis, Paper Endopeptidases / metabolism* Glycine / analogs & derivatives*, analysis Gonadotropin-Releasing Hormone / antagonists & inhibitors* Hydrolysis Proline Oxidase / biosynthesis Rabbits |
| Chemical | |
Reg. No./Substance:
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33515-09-2/Gonadotropin-Releasing Hormone; 56-40-6/Glycine; 598-41-4/glycine amide; EC 1.5.3.-/Proline Oxidase; EC 3.4.-/Endopeptidases; EC 3.4.22.-/Cysteine Endopeptidases; EC 3.4.22.-/endopeptidase B |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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