The use of radioiodinated protein substrates for the assay of trypsin and the hatching enzyme from the amphibian Xenopus laevis
| ISSN: |
0003-2697
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| Source: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
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| Topics: |
Biology
Chemistry and Pharmacology
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| Type of Medium: |
Electronic Resource
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| URL: |
| _version_ | 1798292438341648386 |
|---|---|
| autor | Urch, U.A. Nishihara, T. Hedrick, J.L. |
| autorsonst | Urch, U.A. Nishihara, T. Hedrick, J.L. |
| book_url | http://dx.doi.org/10.1016/0003-2697(79)90240-9 |
| datenlieferant | nat_lic_papers |
| fussnote | Assays for a protease in tissue or cell extracts using synthetic substrates (esters and amides) are often compromised by the presence of nonspecific and non-protease-associated esterase and amidase activities. In addition, substrate specificity for some proteases is dependent on structural aspects of the substrate, so-called secondary specificity sites. The above limitations were present in our attempts to assay and isolate the hatching enzyme from embryos of Xenopus laevis. We developed an assay for the hatching enzyme using ^1^2^5I-labeled fertilization envelopes, the natural substrate for this enzyme. Iodination was accomplished using lactoperoxidase. To test for the general usefulness of the assay and to compare this assay with previously employed ones, the trypsin-catalyzed hydrolysis of ^1^2^5I-labeled hemoglobin was also studied. |
| hauptsatz | hsatz_simple |
| identnr | NLZ183972457 |
| issn | 0003-2697 |
| journal_name | Analytical Biochemistry |
| materialart | 1 |
| package_name | Elsevier |
| publikationsort | Amsterdam |
| publisher | Elsevier |
| reference | 100 (1979), S. 352-356 |
| search_space | articles |
| shingle_author_1 | Urch, U.A. Nishihara, T. Hedrick, J.L. |
| shingle_author_2 | Urch, U.A. Nishihara, T. Hedrick, J.L. |
| shingle_author_3 | Urch, U.A. Nishihara, T. Hedrick, J.L. |
| shingle_author_4 | Urch, U.A. Nishihara, T. Hedrick, J.L. |
| shingle_catch_all_1 | Urch, U.A. Nishihara, T. Hedrick, J.L. The use of radioiodinated protein substrates for the assay of trypsin and the hatching enzyme from the amphibian Xenopus laevis 0003-2697 00032697 Elsevier |
| shingle_catch_all_2 | Urch, U.A. Nishihara, T. Hedrick, J.L. The use of radioiodinated protein substrates for the assay of trypsin and the hatching enzyme from the amphibian Xenopus laevis 0003-2697 00032697 Elsevier |
| shingle_catch_all_3 | Urch, U.A. Nishihara, T. Hedrick, J.L. The use of radioiodinated protein substrates for the assay of trypsin and the hatching enzyme from the amphibian Xenopus laevis 0003-2697 00032697 Elsevier |
| shingle_catch_all_4 | Urch, U.A. Nishihara, T. Hedrick, J.L. The use of radioiodinated protein substrates for the assay of trypsin and the hatching enzyme from the amphibian Xenopus laevis 0003-2697 00032697 Elsevier |
| shingle_title_1 | The use of radioiodinated protein substrates for the assay of trypsin and the hatching enzyme from the amphibian Xenopus laevis |
| shingle_title_2 | The use of radioiodinated protein substrates for the assay of trypsin and the hatching enzyme from the amphibian Xenopus laevis |
| shingle_title_3 | The use of radioiodinated protein substrates for the assay of trypsin and the hatching enzyme from the amphibian Xenopus laevis |
| shingle_title_4 | The use of radioiodinated protein substrates for the assay of trypsin and the hatching enzyme from the amphibian Xenopus laevis |
| sigel_instance_filter | dkfz geomar wilbert ipn albert fhp |
| source_archive | Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
| timestamp | 2024-05-06T08:48:31.816Z |
| titel | The use of radioiodinated protein substrates for the assay of trypsin and the hatching enzyme from the amphibian Xenopus laevis |
| titel_suche | The use of radioiodinated protein substrates for the assay of trypsin and the hatching enzyme from the amphibian Xenopus laevis Assays for a protease in tissue or cell extracts using synthetic substrates (esters and amides) are often compromised by the presence of nonspecific and non-protease-associated esterase and amidase activities. In addition, substrate specificity for some proteases is dependent on structural aspects of the substrate, so-called secondary specificity sites. The above limitations were present in our attempts to assay and isolate the hatching enzyme from embryos of Xenopus laevis. We developed an assay for the hatching enzyme using ^1^2^5I-labeled fertilization envelopes, the natural substrate for this enzyme. Iodination was accomplished using lactoperoxidase. To test for the general usefulness of the assay and to compare this assay with previously employed ones, the trypsin-catalyzed hydrolysis of ^1^2^5I-labeled hemoglobin was also studied. |
| topic | W V |
| uid | nat_lic_papers_NLZ183972457 |