Isolation and characterization of the hatching enzyme from the amphibian, Xenopus laevis
| ISSN: |
0003-9861
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|---|---|
| Source: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
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| Topics: |
Biology
Chemistry and Pharmacology
Physics
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| Type of Medium: |
Electronic Resource
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| URL: |
| _version_ | 1798292188715548672 |
|---|---|
| autor | Urch, U.A. Hedrick, J.L. |
| autorsonst | Urch, U.A. Hedrick, J.L. |
| book_url | http://dx.doi.org/10.1016/0003-9861(81)90110-7 |
| datenlieferant | nat_lic_papers |
| fussnote | The proteolytic activity released at the time of Xenopus laevis embryo hatching, termed the hatching enzyme, was purified and characterized in terms of its physical and enzymatic properties. Using predominantly isoelectric focusing and preparative ultracentrifugation, the enzyme was purified 2200-fold over the starting crude hatching media. From disc gel electrophoretic experiments, the most highly purified form of the enzyme had two enzymatically active charge isomers present with molecular weights of 62,500. With time, the purified enzyme gave rise to a family of enzymatically active charge isomeric proteins. The enzymatic activity of hatching enzyme toward its ^1^2^5I-labeled natural substrate, the fertilization envelope, was optimal at pH 7.7 and was ionic strength dependent. The enzyme was inhibited by Zn^2^+ and by EDTA. From inhibition by the site-specific reagents diisopropylfluorophosphate and phenylmethylsulfonylfluoride, we concluded that the enzyme was of the serine protease type, although its inhibition by Zn^2^+ and EDTA prevents a clear and unequivocal classification of the protease. This enzyme is different from the hatching enzymes reported in fish and echinoderms, on the basis of size, but it is similar to that described in Rana chensinensis on the basis of size and specificity. |
| hauptsatz | hsatz_simple |
| identnr | NLZ18337133X |
| issn | 0003-9861 |
| journal_name | Archives of Biochemistry and Biophysics |
| materialart | 1 |
| package_name | Elsevier |
| publikationsort | Amsterdam |
| publisher | Elsevier |
| reference | 206 (1981), S. 424-431 |
| search_space | articles |
| shingle_author_1 | Urch, U.A. Hedrick, J.L. |
| shingle_author_2 | Urch, U.A. Hedrick, J.L. |
| shingle_author_3 | Urch, U.A. Hedrick, J.L. |
| shingle_author_4 | Urch, U.A. Hedrick, J.L. |
| shingle_catch_all_1 | Urch, U.A. Hedrick, J.L. Isolation and characterization of the hatching enzyme from the amphibian, Xenopus laevis 0003-9861 00039861 Elsevier |
| shingle_catch_all_2 | Urch, U.A. Hedrick, J.L. Isolation and characterization of the hatching enzyme from the amphibian, Xenopus laevis 0003-9861 00039861 Elsevier |
| shingle_catch_all_3 | Urch, U.A. Hedrick, J.L. Isolation and characterization of the hatching enzyme from the amphibian, Xenopus laevis 0003-9861 00039861 Elsevier |
| shingle_catch_all_4 | Urch, U.A. Hedrick, J.L. Isolation and characterization of the hatching enzyme from the amphibian, Xenopus laevis 0003-9861 00039861 Elsevier |
| shingle_title_1 | Isolation and characterization of the hatching enzyme from the amphibian, Xenopus laevis |
| shingle_title_2 | Isolation and characterization of the hatching enzyme from the amphibian, Xenopus laevis |
| shingle_title_3 | Isolation and characterization of the hatching enzyme from the amphibian, Xenopus laevis |
| shingle_title_4 | Isolation and characterization of 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 | 2024-05-06T08:44:33.605Z |
| titel | Isolation and characterization of the hatching enzyme from the amphibian, Xenopus laevis |
| titel_suche | Isolation and characterization of the hatching enzyme from the amphibian, Xenopus laevis The proteolytic activity released at the time of Xenopus laevis embryo hatching, termed the hatching enzyme, was purified and characterized in terms of its physical and enzymatic properties. Using predominantly isoelectric focusing and preparative ultracentrifugation, the enzyme was purified 2200-fold over the starting crude hatching media. From disc gel electrophoretic experiments, the most highly purified form of the enzyme had two enzymatically active charge isomers present with molecular weights of 62,500. With time, the purified enzyme gave rise to a family of enzymatically active charge isomeric proteins. The enzymatic activity of hatching enzyme toward its ^1^2^5I-labeled natural substrate, the fertilization envelope, was optimal at pH 7.7 and was ionic strength dependent. The enzyme was inhibited by Zn^2^+ and by EDTA. From inhibition by the site-specific reagents diisopropylfluorophosphate and phenylmethylsulfonylfluoride, we concluded that the enzyme was of the serine protease type, although its inhibition by Zn^2^+ and EDTA prevents a clear and unequivocal classification of the protease. This enzyme is different from the hatching enzymes reported in fish and echinoderms, on the basis of size, but it is similar to that described in Rana chensinensis on the basis of size and specificity. |
| topic | W V U |
| uid | nat_lic_papers_NLZ18337133X |