Comparison of anionic with cationic peroxidase from cultured peanut cells
| ISSN: |
1573-5044
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|---|---|
| Keywords: |
Arachis hypogaea ; composition ; isozymes ; peroxidase ; synthesis
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| Source: |
Springer Online Journal Archives 1860-2000
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| Topics: |
Biology
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| Notes: |
Abstract A cationic and an anionic peanut peroxidase were isolated to purity as shown by 2D electrophoresis. Amino acid analysis offered evidence for differences. Variations between the isozymes were also noted in a slight difference in the heme absorption maxima, specific enzyme activity and particularly in the relative amount of each in the suspension medium measured by the heme absorption. In contrast the two isozymes were at least partially similar in their structure as demonstrated by the crossreaction with the antisera. The percent crossreactions were used in turn to amend the calculation for the synthetic rate of each isozyme. In spite of the difference in amount secreted in the suspension medium, the in vivo biosynthetic rate of the two isozyme measured cellularly is much the same.
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| Type of Medium: |
Electronic Resource
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| URL: |
| _version_ | 1798296801254572032 |
|---|---|
| autor | Krol, C. Hu M. Huystee, R. B. |
| autorsonst | Krol, C. Hu M. Huystee, R. B. |
| book_url | http://dx.doi.org/10.1007/BF00043700 |
| datenlieferant | nat_lic_papers |
| hauptsatz | hsatz_simple |
| identnr | NLM196025907 |
| issn | 1573-5044 |
| journal_name | Plant cell, tissue and organ culture |
| materialart | 1 |
| notes | Abstract A cationic and an anionic peanut peroxidase were isolated to purity as shown by 2D electrophoresis. Amino acid analysis offered evidence for differences. Variations between the isozymes were also noted in a slight difference in the heme absorption maxima, specific enzyme activity and particularly in the relative amount of each in the suspension medium measured by the heme absorption. In contrast the two isozymes were at least partially similar in their structure as demonstrated by the crossreaction with the antisera. The percent crossreactions were used in turn to amend the calculation for the synthetic rate of each isozyme. In spite of the difference in amount secreted in the suspension medium, the in vivo biosynthetic rate of the two isozyme measured cellularly is much the same. |
| package_name | Springer |
| publikationsjahr_anzeige | 1990 |
| publikationsjahr_facette | 1990 |
| publikationsjahr_intervall | 8009:1990-1994 |
| publikationsjahr_sort | 1990 |
| publisher | Springer |
| reference | 22 (1990), S. 65-70 |
| schlagwort | Arachis hypogaea composition isozymes peroxidase synthesis |
| search_space | articles |
| shingle_author_1 | Krol, C. Hu M. Huystee, R. B. |
| shingle_author_2 | Krol, C. Hu M. Huystee, R. B. |
| shingle_author_3 | Krol, C. Hu M. Huystee, R. B. |
| shingle_author_4 | Krol, C. Hu M. Huystee, R. B. |
| shingle_catch_all_1 | Krol, C. Hu M. Huystee, R. B. Comparison of anionic with cationic peroxidase from cultured peanut cells Arachis hypogaea composition isozymes peroxidase synthesis Arachis hypogaea composition isozymes peroxidase synthesis Abstract A cationic and an anionic peanut peroxidase were isolated to purity as shown by 2D electrophoresis. Amino acid analysis offered evidence for differences. Variations between the isozymes were also noted in a slight difference in the heme absorption maxima, specific enzyme activity and particularly in the relative amount of each in the suspension medium measured by the heme absorption. In contrast the two isozymes were at least partially similar in their structure as demonstrated by the crossreaction with the antisera. The percent crossreactions were used in turn to amend the calculation for the synthetic rate of each isozyme. In spite of the difference in amount secreted in the suspension medium, the in vivo biosynthetic rate of the two isozyme measured cellularly is much the same. 1573-5044 15735044 Springer |
| shingle_catch_all_2 | Krol, C. Hu M. Huystee, R. B. Comparison of anionic with cationic peroxidase from cultured peanut cells Arachis hypogaea composition isozymes peroxidase synthesis Arachis hypogaea composition isozymes peroxidase synthesis Abstract A cationic and an anionic peanut peroxidase were isolated to purity as shown by 2D electrophoresis. Amino acid analysis offered evidence for differences. Variations between the isozymes were also noted in a slight difference in the heme absorption maxima, specific enzyme activity and particularly in the relative amount of each in the suspension medium measured by the heme absorption. In contrast the two isozymes were at least partially similar in their structure as demonstrated by the crossreaction with the antisera. The percent crossreactions were used in turn to amend the calculation for the synthetic rate of each isozyme. In spite of the difference in amount secreted in the suspension medium, the in vivo biosynthetic rate of the two isozyme measured cellularly is much the same. 1573-5044 15735044 Springer |
| shingle_catch_all_3 | Krol, C. Hu M. Huystee, R. B. Comparison of anionic with cationic peroxidase from cultured peanut cells Arachis hypogaea composition isozymes peroxidase synthesis Arachis hypogaea composition isozymes peroxidase synthesis Abstract A cationic and an anionic peanut peroxidase were isolated to purity as shown by 2D electrophoresis. Amino acid analysis offered evidence for differences. Variations between the isozymes were also noted in a slight difference in the heme absorption maxima, specific enzyme activity and particularly in the relative amount of each in the suspension medium measured by the heme absorption. In contrast the two isozymes were at least partially similar in their structure as demonstrated by the crossreaction with the antisera. The percent crossreactions were used in turn to amend the calculation for the synthetic rate of each isozyme. In spite of the difference in amount secreted in the suspension medium, the in vivo biosynthetic rate of the two isozyme measured cellularly is much the same. 1573-5044 15735044 Springer |
| shingle_catch_all_4 | Krol, C. Hu M. Huystee, R. B. Comparison of anionic with cationic peroxidase from cultured peanut cells Arachis hypogaea composition isozymes peroxidase synthesis Arachis hypogaea composition isozymes peroxidase synthesis Abstract A cationic and an anionic peanut peroxidase were isolated to purity as shown by 2D electrophoresis. Amino acid analysis offered evidence for differences. Variations between the isozymes were also noted in a slight difference in the heme absorption maxima, specific enzyme activity and particularly in the relative amount of each in the suspension medium measured by the heme absorption. In contrast the two isozymes were at least partially similar in their structure as demonstrated by the crossreaction with the antisera. The percent crossreactions were used in turn to amend the calculation for the synthetic rate of each isozyme. In spite of the difference in amount secreted in the suspension medium, the in vivo biosynthetic rate of the two isozyme measured cellularly is much the same. 1573-5044 15735044 Springer |
| shingle_title_1 | Comparison of anionic with cationic peroxidase from cultured peanut cells |
| shingle_title_2 | Comparison of anionic with cationic peroxidase from cultured peanut cells |
| shingle_title_3 | Comparison of anionic with cationic peroxidase from cultured peanut cells |
| shingle_title_4 | Comparison of anionic with cationic peroxidase from cultured peanut cells |
| sigel_instance_filter | dkfz geomar wilbert ipn albert fhp |
| source_archive | Springer Online Journal Archives 1860-2000 |
| timestamp | 2024-05-06T09:57:51.815Z |
| titel | Comparison of anionic with cationic peroxidase from cultured peanut cells |
| titel_suche | Comparison of anionic with cationic peroxidase from cultured peanut cells |
| topic | W |
| uid | nat_lic_papers_NLM196025907 |