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| DOI: | 10.1104/pp.61.5.718 |
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| Web URL(s): | http://www.plantphysiol.org/content/61/5/718.full.pdf+html
Last checked: 08/09/12
Requires: PDF Reader
Access conditions: Item is within a limited-access website |
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| Publication Type:
| Refereed |
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| Author(s): | Ashton, Anthony R.;
Polya, Gideon M. |
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| Author Affiliation: | Department of Biochemistry, La Trobe University, Bundoora, Victoria, Australia |
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| Title: | Cyclic adenosine 3':5'-monophosphate in axenic rye grass endosperm cell cultures |
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| Source: | Plant Physiology. Vol. 61, No. 5, May 1978, p. 718-722. |
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| # of Pages: | 5 |
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| Related Web URL: | http://www.plantphysiol.org/content/61/5/718.abstract
Last checked: 08/09/12
Notes: Abstract only |
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| Keywords: | TIC Keywords: Lolium multiflorum; Plant physiology; Dilution; Thin layer chromatography
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| Geographic Terms: | Australia, Victoria |
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| Abstract/Contents: | "Cyclic adenosine 3':5'-monophosphate (cAMP) was extensively purified from rye grass (Lolium multiflorum) endosperm cells grown in axenic suspension culture. The cAMP was purified by neutral alumina and anion and cation exchange chromatography. The cAMP was quantitated by means of a radiochemical saturation assay using a beef heart cAMP-binding protein and also by an assay involving activation of beef heart protein kinase. The cAMP levels found (corrected for recovery of tracer cyclic 3',5'-[8-3H]MP included from the point of sample extraction) ranged from 2 to 12 pmol/g fresh weight. The material purified from rye grass cultures was indistinguishable from authentic cAMP with respect to chromatography in two cellulose thin layer systems, behavior on dilution in both the saturation and protein kinase activation assays, and rates of degradation by a mammalian cAMP phosphodiesterase. The cAMP from rye grass cultures was completely degraded by a mammalian cAMP phosphodiesterase, and 1-methyl-3-isobutylxanthine inhibited such degradation. The protein kinase activation and saturation assays gave essentially the same values for the cAMP content of axenic rye grass culture extracts. Material satisfying the above criteria for identity with cAMP was also isolated from the culture medium. The increase observed in medium cAMP levels during culture growth provides evidence for the synthesis and secretion of cAMP by rye grass endosperm cells in suspension culture." |
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| Language: | English |
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| References: | 24 |
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| Note: | Graphs |
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| ASA/CSSA/SSSA Citation (Crop Science-Like - may be incomplete):
Ashton, A. R., and G. M. Polya. 1978. Cyclic adenosine 3':5'-monophosphate in axenic rye grass endosperm cell cultures. Plant Physiol. 61(5):p. 718-722. |
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| DOI: 10.1104/pp.61.5.718 |
| Web URL(s):
http://www.plantphysiol.org/content/61/5/718.full.pdf+html
Last checked: 08/09/12
Requires: PDF Reader
Access conditions: Item is within a limited-access website |
| 
MSU catalog number: QK 1 .P68 |
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