Multiple forms of human adenosine deaminase. II. Isolation and properties of a conversion factor from human lung
| ISSN: |
0005-2744
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|---|---|
| Source: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
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| Topics: |
Biology
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| Type of Medium: |
Electronic Resource
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| URL: |
| _version_ | 1798292372746928130 |
|---|---|
| autor | Nishihara, H. Ishikawa, S. Shinkai, K. Akedo, H. |
| autorsonst | Nishihara, H. Ishikawa, S. Shinkai, K. Akedo, H. |
| book_url | http://linkinghub.elsevier.com/retrieve/pii/0005-2744(73)90172-1 |
| datenlieferant | nat_lic_papers |
| fussnote | 1. A conversion factor, which can convert the small form (E"S; 47 000 mol. wt) of human adenosine deaminase (EC 3.5.4.4) to the large form (E"L; 230 000 mol. wt), was purified about 600-fold from normal human lung by (NH"4)"2SO"4 fractionation, Sephadex and DEAE-cellulose chromatography, and preparative acrylamide electrophoresis.2. The purified preparation, heat labile and free from the deaminase activity, exhibited upon disc electrophoresis a single protein band associated with the converting activity and also showed a maximum absorption at 280 nm. Its molecular weight was found to be 139 000 when judged by gel filtration with Sephadex G-200.3. The factor did not require sulfhydryl compounds nor bivalent metal ions for exerting its activity.4. Results of quantitative analysis of the rate of formation of E"L from known amounts of conversion factor and E"S, immunochemical characterizations of the two forms of the enzyme in relation to conversion factor by using antiserum against the factor, and polyacrylamide electrophoresis of E"L and the factor in the presence of sodium dodecyl sulfate strongly suggest that E"L is a complex of E"S and conversion factor.5. No detectable activity of conversion factor was demonstrated in an extract of lung cancer tissue. |
| hauptsatz | hsatz_simple |
| identnr | NLZ185783066 |
| issn | 0005-2744 |
| journal_name | BBA - Enzymology |
| materialart | 1 |
| package_name | Elsevier |
| publikationsort | Amsterdam |
| publisher | Elsevier |
| reference | 302 (1973), S. 429-442 |
| search_space | articles |
| shingle_author_1 | Nishihara, H. Ishikawa, S. Shinkai, K. Akedo, H. |
| shingle_author_2 | Nishihara, H. Ishikawa, S. Shinkai, K. Akedo, H. |
| shingle_author_3 | Nishihara, H. Ishikawa, S. Shinkai, K. Akedo, H. |
| shingle_author_4 | Nishihara, H. Ishikawa, S. Shinkai, K. Akedo, H. |
| shingle_catch_all_1 | Nishihara, H. Ishikawa, S. Shinkai, K. Akedo, H. Multiple forms of human adenosine deaminase. II. Isolation and properties of a conversion factor from human lung 0005-2744 00052744 Elsevier |
| shingle_catch_all_2 | Nishihara, H. Ishikawa, S. Shinkai, K. Akedo, H. Multiple forms of human adenosine deaminase. II. Isolation and properties of a conversion factor from human lung 0005-2744 00052744 Elsevier |
| shingle_catch_all_3 | Nishihara, H. Ishikawa, S. Shinkai, K. Akedo, H. Multiple forms of human adenosine deaminase. II. Isolation and properties of a conversion factor from human lung 0005-2744 00052744 Elsevier |
| shingle_catch_all_4 | Nishihara, H. Ishikawa, S. Shinkai, K. Akedo, H. Multiple forms of human adenosine deaminase. II. Isolation and properties of a conversion factor from human lung 0005-2744 00052744 Elsevier |
| shingle_title_1 | Multiple forms of human adenosine deaminase. II. Isolation and properties of a conversion factor from human lung |
| shingle_title_2 | Multiple forms of human adenosine deaminase. II. Isolation and properties of a conversion factor from human lung |
| shingle_title_3 | Multiple forms of human adenosine deaminase. II. Isolation and properties of a conversion factor from human lung |
| shingle_title_4 | Multiple forms of human adenosine deaminase. II. Isolation and properties of a conversion factor from human lung |
| sigel_instance_filter | dkfz geomar wilbert ipn albert fhp |
| source_archive | Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
| timestamp | 2024-05-06T08:47:29.131Z |
| titel | Multiple forms of human adenosine deaminase. II. Isolation and properties of a conversion factor from human lung |
| titel_suche | Multiple forms of human adenosine deaminase. II. Isolation and properties of a conversion factor from human lung 1. A conversion factor, which can convert the small form (E"S; 47 000 mol. wt) of human adenosine deaminase (EC 3.5.4.4) to the large form (E"L; 230 000 mol. wt), was purified about 600-fold from normal human lung by (NH"4)"2SO"4 fractionation, Sephadex and DEAE-cellulose chromatography, and preparative acrylamide electrophoresis.2. The purified preparation, heat labile and free from the deaminase activity, exhibited upon disc electrophoresis a single protein band associated with the converting activity and also showed a maximum absorption at 280 nm. Its molecular weight was found to be 139 000 when judged by gel filtration with Sephadex G-200.3. The factor did not require sulfhydryl compounds nor bivalent metal ions for exerting its activity.4. Results of quantitative analysis of the rate of formation of E"L from known amounts of conversion factor and E"S, immunochemical characterizations of the two forms of the enzyme in relation to conversion factor by using antiserum against the factor, and polyacrylamide electrophoresis of E"L and the factor in the presence of sodium dodecyl sulfate strongly suggest that E"L is a complex of E"S and conversion factor.5. No detectable activity of conversion factor was demonstrated in an extract of lung cancer tissue. |
| topic | W |
| uid | nat_lic_papers_NLZ185783066 |