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. 1973 Jan;51(1):203–209. doi: 10.1104/pp.51.1.203

Comparative Immunochemistry of Phytochrome

Lee H Pratt a
PMCID: PMC367379  PMID: 16658285

Abstract

Partially purified high molecular weight preparations of phytochrome, estimated to be close to 440,000 molecular weight based upon chromatography through a calibrated Bio-Gel P-300 column, were obtained from Garry and Newton oats (Avena Sativa L., cv. Garry and cv. Newton), rye (Secale cereale L., cv. Balbo), barley (Horedum vulgare L., cv. Harrison), and pea (Pisum sativum L., cv. Alaska) by a sequence of three chromatographic steps: brushite, diethylaminoethyl cellulose, and Bio-Gel P-300. No significant differences were observed between these preparations during purification or subsequent handling. In addition, a low molecular weight form of phytochrome was purified from Garry oats. Two specific antisera against a low molecular weight form of phytochrome (60,000 molecular weight) obtained from etiolated Garry oat seedlings are characterized and used to compare the phytochrome preparations. Double diffusion assays indicated antigenic identity between all preparations except that pea phytochrome yielded a spur when compared to oat phytochrome. Micro complement fixation assays yielded complete identity between Garry and Newton oat phytochrome, reduced activity with rye and barley phytochrome, and a complete lack of activity with pea phytochrome at the serum dilutions assayed. Immunoelectrophoretic assays indicated that all high molecular weight phytochrome preparations were homogeneous by this criterion and that there were only slight differences between the preparations in electrophoretic mobility. Large and small forms of phytochrome isolated from Garry oats were found to be very similar antigens when tested with the anti-small phytochrome sera, although the small form was observed to electrophorese at a much slower rate than the large.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Andrews P. The gel-filtration behaviour of proteins related to their molecular weights over a wide range. Biochem J. 1965 Sep;96(3):595–606. doi: 10.1042/bj0960595. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Briggs W. R., Siegelman H. W. Distribution of Phytochrome in Etiolated Seedlings. Plant Physiol. 1965 Sep;40(5):934–941. doi: 10.1104/pp.40.5.934. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Briggs W. R., Zollinger W. D., Platz B. B. Some Properties of Phytochrome Isolated From Dark-grown Oat Seedlings (Avena sativa L.). Plant Physiol. 1968 Aug;43(8):1239–1243. doi: 10.1104/pp.43.8.1239. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Butler W. L., Lane H. C., Siegelman H. W. Nonphotochemical Transformations of Phytochrome in Vivo. Plant Physiol. 1963 Sep;38(5):514–519. doi: 10.1104/pp.38.5.514. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Correll D. L., Edwards J. L. The aggregation States of phytochrome from etiolated rye and oat seedings. Plant Physiol. 1970 Jan;45(1):81–85. doi: 10.1104/pp.45.1.81. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Correll D. L., Steers E., Jr, Towe K. M., Shropshire W., Jr Phytochrome in etiolated annual rye. IV. Physical and chemical characterization of phytochrome. Biochim Biophys Acta. 1968 Sep 10;168(1):46–57. doi: 10.1016/0005-2795(68)90232-8. [DOI] [PubMed] [Google Scholar]
  7. Cundiff S. C., Pratt L. H. Immunological Determination of the Relationship between Large and Small Sizes of Phytochrome. Plant Physiol. 1973 Jan;51(1):210–213. doi: 10.1104/pp.51.1.210. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Gardner G., Pike C. S., Rice H. V., Briggs W. R. "Disaggregation" of phytochrome in vitro-a consequence of proteolysis. Plant Physiol. 1971 Dec;48(6):686–693. doi: 10.1104/pp.48.6.686. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Hopkins D. W., Butler W. L. Immunochemical and spectroscopic evidence for protein conformational changes in phytochrome transformations. Plant Physiol. 1970 May;45(5):567–570. doi: 10.1104/pp.45.5.567. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Mumford F. E., Jenner E. L. Purification and characterization of phytochrome from oat seedlings. Biochemistry. 1966 Nov;5(11):3657–3662. doi: 10.1021/bi00875a039. [DOI] [PubMed] [Google Scholar]
  11. Pike C. S., Briggs W. R. Partial Purification and Characterization of a Phytochrome-degrading Neutral Protease from Etiolated Oat Shoots. Plant Physiol. 1972 Apr;49(4):521–530. doi: 10.1104/pp.49.4.521. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Pratt L. H., Coleman R. A. Immunocytochemical localization of phytochrome. Proc Natl Acad Sci U S A. 1971 Oct;68(10):2431–2435. doi: 10.1073/pnas.68.10.2431. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. SIEGELMAN H. W., FIRER E. M. PURIFICATION OF PHYTOCHROME FROM OAT SEEDLINGS. Biochemistry. 1964 Mar;3:418–423. doi: 10.1021/bi00891a019. [DOI] [PubMed] [Google Scholar]
  14. Walker T. S., Bailey J. L. Studies on phytochrome. Some properties of electrophoretically pure phytochrome. Biochem J. 1970 Dec;120(3):613–622. doi: 10.1042/bj1200613. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Walker T. S., Bailey J. L. Studies on phytochrome. Two photoreversible chromoproteins from etiolated oat seedlings. Biochem J. 1970 Dec;120(3):607–612. doi: 10.1042/bj1200607. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]

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