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- Publisher Website: 10.1016/0020-711X(87)90139-X
- Scopus: eid_2-s2.0-0023070704
- PMID: 3609445
- WOS: WOS:A1987H749500009
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Article: Ornithine decarboxylase from Tetrahymena thermophila: Purification, reversible modification and multiple forms
Title | Ornithine decarboxylase from Tetrahymena thermophila: Purification, reversible modification and multiple forms |
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Authors | |
Issue Date | 1987 |
Citation | International Journal Of Biochemistry, 1987, v. 19 n. 6, p. 545-550 How to Cite? |
Abstract | 1. 1. T. thermophila ornithine decarboxylase was purified 1100-fold by an improved procedure to a specific activity of 2.31 × 10 4 nmol/hr/mg protein with a 28% yield. 2. 2. The purified enzyme was a monomer of M r = 68, 000 and had two isoelectric forms with pI's of 5.14 and 5.17 respectively. 3. 3. The M r = 68, 000 enzyme was reversibly modified by a cellular factor of approx. M r = 10, 000 to give rise to two additional forms with decreased DEAE-cellulose affinity. © 1987. |
Persistent Identifier | http://hdl.handle.net/10722/147320 |
ISSN | |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Yao, KM | en_US |
dc.contributor.author | Fong, WF | en_US |
dc.date.accessioned | 2012-05-29T06:02:54Z | - |
dc.date.available | 2012-05-29T06:02:54Z | - |
dc.date.issued | 1987 | en_US |
dc.identifier.citation | International Journal Of Biochemistry, 1987, v. 19 n. 6, p. 545-550 | en_US |
dc.identifier.issn | 0020-711X | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/147320 | - |
dc.description.abstract | 1. 1. T. thermophila ornithine decarboxylase was purified 1100-fold by an improved procedure to a specific activity of 2.31 × 10 4 nmol/hr/mg protein with a 28% yield. 2. 2. The purified enzyme was a monomer of M r = 68, 000 and had two isoelectric forms with pI's of 5.14 and 5.17 respectively. 3. 3. The M r = 68, 000 enzyme was reversibly modified by a cellular factor of approx. M r = 10, 000 to give rise to two additional forms with decreased DEAE-cellulose affinity. © 1987. | en_US |
dc.language | eng | en_US |
dc.relation.ispartof | International Journal of Biochemistry | en_US |
dc.title | Ornithine decarboxylase from Tetrahymena thermophila: Purification, reversible modification and multiple forms | en_US |
dc.type | Article | en_US |
dc.identifier.email | Yao, KM:kmyao@hku.hk | en_US |
dc.identifier.authority | Yao, KM=rp00344 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1016/0020-711X(87)90139-X | - |
dc.identifier.pmid | 3609445 | - |
dc.identifier.scopus | eid_2-s2.0-0023070704 | en_US |
dc.identifier.volume | 19 | en_US |
dc.identifier.issue | 6 | en_US |
dc.identifier.spage | 545 | en_US |
dc.identifier.epage | 550 | en_US |
dc.identifier.isi | WOS:A1987H749500009 | - |
dc.identifier.scopusauthorid | Yao, KM=7403234578 | en_US |
dc.identifier.scopusauthorid | Fong, WF=24433413900 | en_US |
dc.identifier.issnl | 0020-711X | - |