Accession Number
      038057883
Authors
      Yuan W.
Institution
      DEP. PLANT PATHOL. PHYSIOL., CLEMSON UNIV., CLEMSON, S.C. 29634.
Title
      SELECTIVE CHEMICALS FOR ISOLATION OF XANTHOMONAS-CAMPESTRIS PATHOVAR ORYZAE ISHIYAMA DYE.
Source
      ANNUAL MEETING OF THE AMERICAN PHYTOPATHOLOGICAL SOCIETY, RICHMOND, VIRGINIA, USA, AUGUST 20-24, 1989. Phytopathology 79 (10). 1989.
      1191.
Year of Publication
      1989
Publication Type
      Meeting.
ISSN
      0031-949X
Keywords
      ABSTRACT.
Concept Codes
      *Microbiological Apparatus, Methods and Media [32000]
      *Phytopathology / Diseases Caused by Bacteria [54504]
      General Biology / Symposia, Transactions and Proceedings of Conferences, Congresses, Review Annuals [00520]
Biosystematic Codes/Super Taxa
      Pseudomonadaceae (1979-91) [04716]
      Microorganisms. Bacteria.
Languages
      English.
Abstrate
      Cephradine (40 ug/ml), cephaloridine (1 ug/ml), crystal violet (4 ug/ml), methyl violet (3 ug/ml) and nalidixic acid (4 ug/ml) all permitted growth of Xanthomonas campestris pv. oryzae (Ishiyama) Dye in liquid media and were tested separately by replica plating with 5 Chinese and two IRRI (PSC-79 & PXO-86) strains of X. c. oryzae and 34 bacteria from rice seeds.  All chemicals permitted growth of all X. c. oryzae strains.  Crystal violet inhibited all 7 Gram-positives, 7 of 17 non-yellow, Gram-negatives, and 1 of 7 yellow, oxidative, Gram-negatives while methyl violet inhibited 4 of the same Gram-positives and 4 of the same non-yellow, Gram-negatives. Nalidixic acid (1 ug/ml) inhibited all 3 yellow, fermentative, Gram-negatives.  Cephradine inhibited 7 non-yellow, Gram-negatives and 5 Gram-positives while cephaloridine inhibited 4 of the same non-yellow, Gram-negatives and 3 of the same Gram-positives.  Five yellow, oxidative, Gram negatives were not suppressed by the chemicals.  Cycloheximide (>100 ug/ml) inhibited X. c. oryzae.  Combinations of chemicals should be tested for isolation of X. c. oryzae.
Entry Week
      9000


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Accession Number
      039054070
Authors
      Yuan W. Hooten C D. Lezica R P. Showalter A M.
Institution
      BOTANY DEP., MOL. AND CELLULAR BIOL. PROGRAM, OHIO UNIV., ATHENS, GA. 45701.
Title
      CLONING AND CHARACTERIZATION OF COMPLEMENTARY DNA ENCODING POTATO TUBER LECTIN AND EXTENSIN.
Source
      ANNUAL MEETING OF THE AMERICAN SOCIETY OF PLANT PHYSIOLOGISTS, INDIANAPOLIS, INDIANA, USA, JULY 29-AUGUST 2, 1990. Plant Physiology
      (Bethesda) 93 (1 Suppl.). 1990. 42.
Year of Publication
      1990
Publication Type
      Meeting.
ISSN
      0032-0889
Keywords
      ABSTRACT.
Concept Codes
      *Genetics and Cytogenetics / Plant [03504]
      *Biochemical Studies / Nucleic Acids, Purines and Pyrimidines [10062]
      *Biophysics / Molecular Properties and Macromolecules [10506]
      *Metabolism / Carbohydrates [13004]
      *Metabolism / Proteins, Peptides and Amino Acids [13012]
      *Plant Physiology, Biochemistry and Biophysics / Metabolism [51519]
      General Biology / Symposia, Transactions and Proceedings of Conferences, Congresses, Review Annuals [00520]
      Biochemical Studies / Proteins, Peptides and Amino Acids [10064]
      Biochemical Studies / Carbohydrates [10068]
Biosystematic Codes/Super Taxa
      Solanaceae [26775]
      Plants. Vascular Plants. Spermatophytes. Angiosperms. Dicots.
Languages
      English.
Abstrate
      The solanaceous lectins represent a class of plant hydroxyproline glycoproteins which bind oligomers of N-acetylglucosamine.  Potato tuber lectin (PTL) has been found in potato tuber and is biochemically the best studied of the solanaceous lectins.  Potato tuber lectin consists of two distinct domains: 1) a glycosylated domain, like plant cell wall extensin, rich in hydroxyproline (Hyp) and serine with 1-4 arabinoses linked to Hyp and 1 to 2 galactoses O-linked to serine and 2) a non-glycosylated domain, like wheat germ agglutinin (WGA) and other potato cysteine-rich proteins, rich in glycine and cysteine and capable of binding oligomers of N-acetylglucosamine.  These lectins are thought to function in cell-cell recognition, wound healing, and plant defense since N-acetylgluco-samine is a major component of cell wall.  No amino acid sequences nor gene information for the hydroxyproline-rich solanaceous lectins are published.  We are trying to isolate and characterize potato tuber lectin cDNA clones.  This research will provide preliminary materials and information necessary for further isolation of plant genes encoding this group of lectins and related proteins such as some cysteine-rich phloem proteins, for studies on regulation of these genes, and for the investigation of solanaceous lectin function via genetic engineering approaches.
Entry Week
      9000


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