Skip to main content
NCBI home page
Plant Physiology logoLink to Plant Physiology
. 1982 Jan;69(1):268–272. doi: 10.1104/pp.69.1.268

Cytoplasmic Male Sterility in Barley 1

VIII. LIPOXYGENASE ACTIVITY AND ANTHER AMINO NITROGEN IN THE msm1-Rfm1a SYSTEM

Hannu Ahokas 1
PMCID: PMC426187  PMID: 16662173

Abstract

The lipoxygenase (LOX) activity was determined in almost isogenic types of barley (Hordeum vulgare L.): normal cv. Adorra, cytoplasmic male sterile (msm1), and msm1 barley with restored fertility, heterozygous for the Rfm1a restorer gene. The LOX activity was lowest in male steriles in the leaf tissue studied at the anthesis stage. The LOX activity in developing anthers was higher than in leaf tissue, and decreased during degeneration of the sterile anthers.

On polyacrylamide gel electrophoresis slabs, the LOX of anther homogenates moved in a complex which evidently carried some lipid and pigment, too. The LOX zones showed pseudoisoenzymic movement, i.e. a gradual increase in mobility dependent on the age of the anthers. On sodium dodecyl sulfate-polyacrylamide gel electrophoresis slabs, the LOX zones contained three polypeptides. When sporopollenin production ends in the fertile anthers, a fourth polypeptide (molecular weight 91,200) appears in their LOX zones. This `late' polypeptide is missing from steriles, and is suggested as being associated with the termination of sporopollenin production in the tapetum of fertiles.

Sterile anthers were found to be almost devoid of soluble NH2-N, which supports the idea of their starvation. This starvation can reasonably be held responsible for the absence of late proteins (e.g. the 91,200 dalton polypeptide), and is reinforced by the uncontrolled production of sporopollenin.

Full text

PDF
268

Images in this article

270Image
on p.270
271Image
on p.271

Selected References

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

  1. Arens D., Seilmeier W., Weber F., Kloos G., Grosch W. Purification and properties of a carotene co-oxidizing lipoxygenase from peas. Biochim Biophys Acta. 1973 Dec 19;327(2):295–305. doi: 10.1016/0005-2744(73)90412-9. [DOI] [PubMed] [Google Scholar]
  2. Arnon D. I. COPPER ENZYMES IN ISOLATED CHLOROPLASTS. POLYPHENOLOXIDASE IN BETA VULGARIS. Plant Physiol. 1949 Jan;24(1):1–15. doi: 10.1104/pp.24.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Beaux Y., Drapron R., Nicolas J., Caillat J. M. La lipoxygénase de la fève (Vicia faba L.) I. Isolement. Biochimie. 1973;55(3):253–262. doi: 10.1016/s0300-9084(73)80123-3. [DOI] [PubMed] [Google Scholar]
  4. Camm E. L., Green B. R. Fractionation of Thylakoid Membranes with the Nonionic Detergent Octyl-beta-d-glucopyranoside: RESOLUTION OF CHLOROPHYLL-PROTEIN COMPLEX II INTO TWO CHLOROPHYLL-PROTEIN COMPLEXES. Plant Physiol. 1980 Sep;66(3):428–432. doi: 10.1104/pp.66.3.428. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  6. DeLumen B. O., Kazeniac S. J. Staining for lipoxygenase activity in electrophoretic gels. Anal Biochem. 1976 May 7;72:428–432. doi: 10.1016/0003-2697(76)90550-9. [DOI] [PubMed] [Google Scholar]
  7. Eriksson C. E., Svensson S. G. Lipoxygenase from peas, purification and properties of the enzyme. Biochim Biophys Acta. 1970 Mar 18;198(3):449–459. doi: 10.1016/0005-2744(70)90123-3. [DOI] [PubMed] [Google Scholar]
  8. Grosch W., Laskawy G. Co-oxidation of carotenes requires one soybean lipoxygenase isoenzyme. Biochim Biophys Acta. 1979 Dec 18;575(3):439–445. doi: 10.1016/0005-2760(79)90113-9. [DOI] [PubMed] [Google Scholar]
  9. Grossman S., Zakut R. Determination of the activity of lipoxygenase (lipoxidase). Methods Biochem Anal. 1979;25:303–329. doi: 10.1002/9780470110454.ch5. [DOI] [PubMed] [Google Scholar]
  10. Markwell J. P., Thornber J. P., Boggs R. T. Higher plant chloroplasts: Evidence that all the chlorophyll exists as chlorophyll-protein complexes. Proc Natl Acad Sci U S A. 1979 Mar;76(3):1233–1235. doi: 10.1073/pnas.76.3.1233. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Ramadoss C. S., Pistorius E. K., Axelrod B. Coupled oxidation of carotene by lipoxygenase requires two isoenzymes. Arch Biochem Biophys. 1978 Oct;190(2):549–552. doi: 10.1016/0003-9861(78)90309-0. [DOI] [PubMed] [Google Scholar]
  12. Schneeberger E. E., Lynch R. D., Geyer R. P. Formation and disappearance of triglyceride droplets in strain L fibroblasts. An electron microscopic study. Exp Cell Res. 1971 Nov;69(1):193–206. doi: 10.1016/0014-4827(71)90325-9. [DOI] [PubMed] [Google Scholar]
  13. Spaapen L. J., Verhagen J., Veldink G. A., Vliegenthart J. F. The effect of modification of sulfhydryl groups in soybean lipoxygenase-1. Biochim Biophys Acta. 1980 Apr 18;618(1):153–162. doi: 10.1016/0005-2760(80)90062-4. [DOI] [PubMed] [Google Scholar]
  14. WADDELL W. J. A simple ultraviolet spectrophotometric method for the determination of protein. J Lab Clin Med. 1956 Aug;48(2):311–314. [PubMed] [Google Scholar]
  15. 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]
  16. de la Roche A. I. Increase in linolenic Acid is not a prerequisite for development of freezing tolerance in wheat. Plant Physiol. 1979 Jan;63(1):5–8. doi: 10.1104/pp.63.1.5. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES