Plant Physiology

Cane, Alan R.; Wilkins, Malcolm B.

doi: 10.1104/pp.44.11.1481pmid: 16657231

Abstract The possible interdependence of the differential longitudinal, and the lateral movement of indoleacetic acid (IAA) in horizontal Zea coleoptile segments has been examined. The coleoptiles have been opened out into flat pieces of tissue and supplied apically with IAA-1-14C. Opened-out segments orientated so that all the cells correspond with those at the `bottom' of a normal horizontal coleoptile, transport more IAA basipetally than do segments in which all the cells are equivalent to those at the `top' of the horizontal coleoptile. In opened-out segments orientated so that all the cells are equivalent to those at the side of the horizontal coleoptile cylinder, there is no difference in the basipetal transport capacity of the upper and lower halves. This is so even if the tissue has been in the horizontal position for 90 min before being bisected into its upper and lower halves. In this `side' tissue, however, there is a polarized downward movement of IAA. At least 95% of the 14C in both the upper and lower halves of the tissue is confined to the IAA molecule. In horizontal Zea coleoptiles the polarized lateral movement of IAA can therefore occur independently of the differential basipetal transport of IAA in the upper and lower halves of the organ. This content is only available as a PDF. © 1969 American Society of Plant Biologists This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model)

Ory, Robert L.; Henningsen, Knud W.

doi: 10.1104/pp.44.11.1488pmid: 5397495

Abstract Protein bodies were isolated intact from dormant barley seeds, Hordeum vulgare, var. Kenia, by a combination of buffer extractions and centrifugations over a sucrose gradient. Examination of the protein bodies pellet in the electron microscope shows 2 types of protein bodies in a wide variation of sizes. The majority of them stain evenly with osmium, are contained within a single membrane, and have no other structural components. The other type, mostly the larger particles, has a fine structure of orderly dark and light-stained layers attached to the protein bodies. Two acid hydrolases are associated with these particles: acid phosphatase activity, specific for sodium phytate but inactive on β-glycerol phosphate, glucose 1-phosphate, fructose 1,6-diphosphate and adenosine triphosphate; and acid protease activity. 1 Fulbright-Hayes Research Scholar in Denmark, 1968-69. Permanent address: Southern Regional Research Laboratory, P.O. Box 19687, New Orleans, Louisiana. 70119 U.S.A. Requests for reprints should be sent to Prof. R. J. Djurtoft at the Polytechnic Institute. This content is only available as a PDF. © 1969 American Society of Plant Biologists This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model)

Weinstein, L. H.; McCune, D. C.; Mancini, Jill F.; van Leuken, P.

doi: 10.1104/pp.44.11.1499pmid: 16657232

Abstract Acid-soluble nucleotides of unifoliate leaves of Pinto bean plants (Phaseolus vulgaris L.) were determined at young, mature, and senescent stages of development. At least 25 components could be distinguished on the basis of inorganic phosphorus determinations and 37 or more fractions on the basis of 32P labeling, with adenosine di- and triphosphates accounting for 60% of the total moles of nucleotide. The total nucleotide P and inorganic P, on a fresh weight basis, decreased about 44% between each stage of leaf development, but decrements in the levels of individual nucleotides varied from this over-all pattern. Minor changes in the relative abundance of the individual nucleotides accompanied aging although the percentage of purine-containing nucleotides decreased with age. Total 32P activity per leaf in the nucleotide pool increased about 3-fold between the young and mature leaves and decreased slightly as leaves became senescent. In general, the specific activities of the nucleotides increased with increased age and adenosine-, guanosine-, uridine-, and cytidine triphosphates and adenosine diphosphate accounted for approximately 90% of the total activity. The changes in the relative sizes and energy status of the nucleotide pools were not so obvious as the changes in other metabolites that have been reported to accompany aging in leaf tissue. 1 Supported in part by grant AP-00189 from the National Air Pollution Control Administration, Consumer Protection and Environmental Health Service, United States Public Health Service. This content is only available as a PDF. © 1969 American Society of Plant Biologists This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model)

Forti, Giorgio; Meyer, Emilia Maria

doi: 10.1104/pp.44.11.1511pmid: 16657233

Abstract Inorganic pyrophosphate is found to inhibit the ferredoxin-dependent photoreduction of NADP by isolated chloroplasts. The reduction of ferricyanide is not inhibited, nor is the activity of photosystem 1 as measured with methyl viologen as the electron acceptor. All other ferredoxin-depended reactions are inhibited, such as cytochrome c photoreduction and the reaction sequence: NADPH →Flavoprotein→ferredoxin→cytochrome c. The inhibition by pyrophosphate is, in all cases, competitive with ferredoxin and independent of NADP concentration. Pyrophosphate inhibition of the formation of the ferredoxin-flavoprotein complex is demonstrated spectrophotometrically. This content is only available as a PDF. © 1969 American Society of Plant Biologists This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model)

Howes, Charles D.; Stern, Arthur I.

doi: 10.1104/pp.44.11.1515pmid: 16657234

Abstract Optimal conditions were determined for photophosphorylation and reduction in mature chloroplasts from Phaseolus vulgaris var. Red Kidney. Bovine serum albumin (BSA) at 1 mg/ml and various sulfhydryl reagents (0.1-0.5 mm) greatly enhanced cyclic and noncyclic phosphorylation, but had little effect on photoreduction. BSA and reduced glutathione also stimulated cyclic phosphorylation in spinach chloroplasts. BSA was needed in the reaction from the start to provide high rates of phosphorylation. BSA also protected against atebrin uncoupling but not against uncoupling by ammonium ions or inhibition by 3,-(3,4-dichlorophenyl)-1,1-dimethylurea. Similarly, BSA and glutathione protected against atebrin inhibition of cyclic phosphorylation. Chloroplasts incubated at 0° rapidly lost the ability to catalyze phosphorylation and BSA did not protect against inactivation. 3 Recipient of a NDEA Title IV Fellowship. Present address: Department of Biology, Wright State University, Dayton, Ohio, 45431. 1 This work was supported in part by research grants GB-4591 and GB-7274 from the National Science Foundation. 2 The data are taken from a dissertation submitted by C. D. Howes to the graduate faculty of the University of Massachusetts in partial fulfillment of the requirements for the Ph.D. degree. This content is only available as a PDF. © 1969 American Society of Plant Biologists This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model)

Webster, D. E.; Chang, S. B.

doi: 10.1104/pp.44.11.1523pmid: 5397496

Abstract Two polygalactolipids, designated as components A and B, were isolated from spinach chloroplasts and were also obtained from glycolipid products synthesized with chloroplast enzymes using uridine diphosphate galactose as a galactose donor. These lipids were purified by column and thin layer chromatography. Chemical analysis of component A indicates that the lipid is trigalactosyl diglyceride, whereas component B behaves like tetragalactosyl diglyceride on a thin layer plate. The major fatty acid in trigalactosyl diglyceride was α-linolenic acid. Relative amount (molar ratio) of galactolipids in spinach chloroplasts was monogalactosyl diglyceride:digalactosyl diglyceride:trigalactosyl diglyceride:(tetragalactosyl diglyceride) = 60:30:5:1. 2 To whom all the communications are to be addressed. 1 This work was supported by a grant from NSF (GB-4574). This content is only available as a PDF. © 1969 American Society of Plant Biologists This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model)

Hiatt, A. J.

doi: 10.1104/pp.44.11.1528pmid: 16657235

Abstract Excised roots of barley (Hordeum vulgare, var. Campana) were incubated for 24 hr in solutions containing constant total concentrations of KCl and NaCl but in which the mole fractions of K and Na were varied in replacement series. In solutions containing 1, 10, or 50 mm concentrations of K+ plus Na+, total cation accumulation was dependent upon the total salt concentration but was relatively independent of the mole fractions of K+ and Na+. These results imply that accumulation of K+ and Na+ was limited by a common factor. In solutions containing 0.01 mm K+ plus Na+ there was a strong preference for K+ over Na+ and the sum of K+ and Na+ accumulation increased with increasing K+ concentration. In the replacement series utilizing 0.1 mm K+ plus Na+, K+ accumulation reached a peak at solution concentrations of 0.04 mm K+ and 0.06 mm Na+. Potassium accumulation then decreased as Na+ was further replaced by K+ to concentrations of 0.06 mm K+ and 0.04 mm Na+. Potassium accumulation again increased with additional replacement of Na+ by K+. 1 Contribution (Article No. 69-3-42) of the Department of Agronomy, Kentucky Agricultural Experiment Station, Lexington, and published with approval of the Director. This content is only available as a PDF. © 1969 American Society of Plant Biologists This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model)

Kannangara, C. Gamini

doi: 10.1104/pp.44.11.1533pmid: 16657236

Abstract Ribulose 1,5-diphosphate carboxylase is synthesized in barley leaves growing in the dark. Upon illumination there is a marked increase in the rate of synthesis of the enzyme. The specific activity of the enzyme expressed as cpm incorporated into phosphoglyceric acid per μg of fraction I protein, after isolation shows no change either during dark growth or greening. During early stages of illumination of 7 day dark grown leaves with 320 foot-candles the enzymic activity in the water soluble protein fraction of the leaf shows a short term decline after 15 min which lasts for 30 min. Leaves greening at 2 foot-candles show a similar decline which is shifted to a time between the fourth and eighth hr after the onset of illumination. 1 Research supported by NIH grant and grants from the Danish Research Council and the Carlsberg Foundation to Professor D. von Wettstein. This content is only available as a PDF. © 1969 American Society of Plant Biologists This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model)

Weaver, Ellen C.

doi: 10.1104/pp.44.11.1538pmid: 16657237

Abstract The electron paramagnetic resonance (EPR) characteristics of wild type Chlamydomonas reinhardtii are compared with those of a mutant strain (ac-206) which lacks cytochrome 553. The steady-state signals I and II are similar but differ in their responses to light of long and short wavelengths, reflecting the fact that the electron transport chain linking photosystems I and II is interrupted. The kinetic behavior of signal I is simpler in the mutant, which lacks induction effects prominent in the wild type. The decay of the signal when light ceases is not dependent on the length or intensity of illumination in the mutant, whereas it is in the wild type. These data can be interpreted in terms of signal I being a reflection of cyclic flow in a pathway which does not involve cytochrome 553 in the mutant, whereas in the wild type there is also a contribution of electrons from photosystem II. 1 Paper I of this series is E. C. Weaver, Photochem. Photobiol. 7: 93-100 (1968). This content is only available as a PDF. © 1969 American Society of Plant Biologists This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model)

Kanemasu, E. T.; Tanner, C. B.

doi: 10.1104/pp.44.11.1542pmid: 16657238

Abstract The effect of light on the stomatal resistance of abaxial and adaxial leaf surfaces of snap beans (Phaseolus vulgaris L.) was studied in the growth chamber and in the field. The adaxial stomata required more light to open than the abaxial stomata; the abaxial stomatal apertures were still about 50% open at 1% full sunlight and light-induced closure was never observed under daytime field conditions. A given value of abaxial stomatal resistance was obtained at a given illumination of the abaxial guard cells whether illumination was adaxial or abaxial. 2 Present address: Evapotranspiration Laboratory, Agronomy Department, Kansas State University, Manhattan, Kansas 66502. 1 Paper II precedes Paper I. See page 1547. This content is only available as a PDF. © 1969 American Society of Plant Biologists This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model)