scholarly journals Activity of Meadowfoam (Limnanthes alba) Seed Meal Glucolimnanthin Degradation Products against Soilborne Pathogens

2011 ◽  
Vol 60 (1) ◽  
pp. 339-345 ◽  
Author(s):  
Inga A. Zasada ◽  
Jerry E. Weiland ◽  
Ralph L. Reed ◽  
Jan F. Stevens
Keyword(s):  
Degradation Products ◽  
Seed Meal ◽  
Soilborne Pathogens ◽  
Limnanthes Alba

scholarly journals Herbicidal Activity of Glucosinolate Degradation Products in Fermented Meadowfoam (Limnanthes alba) Seed Meal

2009 ◽  
Vol 57 (5) ◽  
pp. 1821-1826 ◽  
Author(s):  
Jan F. Stevens ◽  
Ralph L. Reed ◽  
Susan Alber ◽  
Larry Pritchett ◽  
Stephen Machado
Keyword(s):  
Degradation Products ◽  
Herbicidal Activity ◽  
Seed Meal ◽  
Limnanthes Alba

Potential of meadowfoam ( Limnanthes alba ) seed meal as an organic source of nitrogen

2018 ◽  
Vol 125 ◽  
pp. 273-277
Author(s):  
Cafer Türkmen ◽  
David D. Myrold
Keyword(s):  
Seed Meal ◽  
Limnanthes Alba ◽  
Organic Source

scholarly journals Characterization of Phytoecdysteroid Glycosides in Meadowfoam (Limnanthes alba) Seed Meal by Positive and Negative Ion LC-MS/MS

2008 ◽  
Vol 56 (11) ◽  
pp. 3945-3952 ◽  
Author(s):  
Jan F. Stevens ◽  
Ralph L. Reed ◽  
Jeffrey T. Morré
Keyword(s):  
Negative Ion ◽  
Seed Meal ◽  
Limnanthes Alba

Field Evaluation of Meadowfoam (Limnanthes alba) Seed Meal for Weed Management

Weed Science ◽  
2015 ◽  
Vol 63 (1) ◽  
pp. 302-311 ◽  
Author(s):  
Suphannika Intanon ◽  
Andrew G. Hulting ◽  
Carol A. Mallory-Smith
Keyword(s):  
Weed Control ◽  
Weed Management ◽  
Untreated Control ◽  
Field Evaluation ◽  
Seed Meal ◽  
Growth Enhancement ◽  
Limnanthes Alba ◽  
Lettuce Yield ◽  
Leaf N Content ◽  
Weed Emergence

Meadowfoam seed meal (MSM), a by-product after oil extraction, has potential uses for crop growth enhancement or weed control. The herbicidal effect of MSM is the result of a secondary metabolite, glucosinolate glucolimnanthin (GLN). Field evaluations were conducted using concentrations of 3, 5, and 7% by weight and two forms (nonactivated and activated) of MSM applied as soil amendments. No injury was observed on lettuce transplanted 7 d after MSM incorporation in 2011. Activated MSM at 7% reduced weed emergence up to 71%. Lettuce leaf N content was at least 8.5-fold greater in MSM treatments compared to the untreated control. Greater soil nitrate levels correlated with greater weed biomass in MSM-amended plots. Isothiocyanate, a potent herbicidal compound, was detected in soil incorporated with 7% activated MSM. In 2012, 2.86 g m−2 of activated MSM, applied as a split or single dose, was evaluated for weed control efficacy and crop injury response. The split MSM application provided weed control similar to that from the single MSM application. The split and single MSM applications inhibited spiny sowthistle emergence more than 95% compared to the untreated control. A single application of activated MSM as a PRE soil amendment suppressed weeds and increased lettuce yield.

scholarly journals Identifying Rates of Meadowfoam (Limnanthes alba) Seed Meal Needed for Suppression of Meloidogyne hapla and Pythium irregulare in Soil

Plant Disease ◽  
2014 ◽  
Vol 98 (9) ◽  
pp. 1253-1260 ◽  
Author(s):  
Yurdagül Şimşek Erşahin ◽  
Jerry E. Weiland ◽  
Inga A. Zasada ◽  
Ralph L. Reed ◽  
J. Fred Stevens
Keyword(s):  
Production Systems ◽  
Seed Meal ◽  
Meloidogyne Hapla ◽  
Pythium Irregulare ◽  
Complete Control ◽  
Limnanthes Alba ◽  
Pathogen Suppression ◽  
Plant Metabolite ◽  
Secondary Plant Metabolite ◽  
Amended Soil

Meadowfoam (Limnanthes alba) is a commercial oilseed annual crop grown in Oregon. After extracting oil from seed, the remaining seed meal is rich in the secondary plant metabolite glucolimnanthin, which can be converted into pesticidal compounds such as 3-methoxybenzyl isothiocyanate (ITC) and 3-methoxyphenylacetonitrile (nitrile) in the presence of the enzyme myrosinase. In previous studies, we demonstrated that ITC and nitrile, produced by mixing freshly ground meadowfoam seed with meadowfoam seed meal, are toxic to the plant-parasitic nematode Meloidogyne hapla and the plant pathogen Pythium irregulare. In this study, we evaluated factors that might influence the implementation of meadowfoam seed meal into agricultural production systems for soilborne pathogen and nematode control. Rate-finding experiments demonstrated that a minimum 1.0% seed/seed meal formulation (wt/wt) was necessary to achieve nematode and pathogen suppression; seed meal alone was insufficient for complete control of M. hapla and stimulated the growth of P. irregulare. When this 1.0% seed/seed meal formulation was used, a greater soil amendment rate was required to cause 100% mortality of P. irregulare (1.0% wt/wt) than for M. hapla (0.5% wt/wt). In phytotoxicity experiments, soil amended with the 1.0% seed/seed meal formulation was consistently phytotoxic to wheat, cucumber, and tomato. However, phytotoxic effects were mitigated by a delayed planting into the amended soil. A final assay to monitor concentrations of ITC and nitrile in conjunction with assessing M. hapla and P. irregulare mortality was conducted over a 6-day period in soils amended at 0.5 and 1.0% (wt/wt) with the 1.0% seed/seed meal formulation. The response was rapid, with 100% mortality of both organisms within 2 h after exposure to amended soil. Concentrations of nitrile remained relatively constant over the 6-day period (approximately 0.017 and 0.032 mg/ml at 0.5 and 1.0% amendment rates, respectively), whereas ITC production increased rapidly and peaked 12 to 24 h after amendment (0.083 and 0.171 mg/ml at 0.5 and 1.0% amendment rates, respectively) before returning to near undetectable levels.

Identification and Phytotoxicity of a New Glucosinolate Breakdown Product from Meadowfoam (Limnanthes alba) Seed Meal

2014 ◽  
Vol 62 (30) ◽  
pp. 7423-7429 ◽  
Author(s):  
Suphannika Intanon ◽  
Ralph L. Reed ◽  
Jan F. Stevens ◽  
Andrew G. Hulting ◽  
Carol A. Mallory-Smith
Keyword(s):  
Seed Meal ◽  
Breakdown Product ◽  
Limnanthes Alba

Collagen degradation products modulate matrix metalloproteinase expression in cultured articular chondrocytes

2005 ◽  
Vol 24 (1) ◽  
pp. 63-70 ◽  
Author(s):  
M. Fichter ◽  
U. Körner ◽  
J. Schömburg ◽  
L. Jennings ◽  
A. A. Cole ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Articular Chondrocytes ◽  
Degradation Products ◽  
Collagen Degradation ◽  
Collagen Degradation Products

Structural Studies of Fibrinolysis by Electron and Light Microscopy

1999 ◽  
Vol 82 (08) ◽  
pp. 277-282 ◽  
Author(s):  
Yuri Veklich ◽  
Jean-Philippe Collet ◽  
Charles Francis ◽  
John W. Weisel
Keyword(s):  
Electron Microscopy ◽  
Light Microscopy ◽  
Plasminogen Activator ◽  
Structural Changes ◽  
Molecular Mechanisms ◽  
Degradation Products ◽  
Molecular Model ◽  
Three Dimensional ◽  
Tissue Type ◽  
Type Plasminogen Activator

IntroductionMuch is known about the fibrinolytic system that converts fibrin-bound plasminogen to the active protease, plasmin, using plasminogen activators, such as tissue-type plasminogen activator (t-PA) and urokinase-type plasminogen activator. Plasmin then cleaves fibrin at specific sites and generates soluble fragments, many of which have been characterized, providing the basis for a molecular model of the polypeptide chain degradation.1-3 Soluble degradation products of fibrin have also been characterized by transmission electron microscopy, yielding a model for their structure.4 Moreover, high resolution, three-dimensional structures of certain fibrinogen fragments has provided a wealth of information that may be useful in understanding how various proteins bind to fibrin and the overall process of fibrinolysis (Doolittle, this volume).5,6 Both the rate of fibrinolysis and the structures of soluble derivatives are determined in part by the fibrin network structure itself. Furthermore, the activation of plasminogen by t-PA is accelerated by the conversion of fibrinogen to fibrin, and this reaction is also affected by the structure of the fibrin. For example, clots made of thin fibers have a decreased rate of conversion of plasminogen to plasmin by t-PA, and they generally are lysed more slowly than clots composed of thick fibers.7-9 Under other conditions, however, clots made of thin fibers may be lysed more rapidly.10 In addition, fibrin clots composed of abnormally thin fibers formed from certain dysfibrinogens display decreased plasminogen binding and a lower rate of fibrinolysis.11-13 Therefore, our increasing knowledge of various dysfibrinogenemias will aid our understanding of mechanisms of fibrinolysis (Matsuda, this volume).14,15 To account for these diverse observations and more fully understand the molecular basis of fibrinolysis, more knowledge of the physical changes in the fibrin matrix that precede solubilization is required. In this report, we summarize recent experiments utilizing transmission and scanning electron microscopy and confocal light microscopy to provide information about the structural changes occurring in polymerized fibrin during fibrinolysis. Many of the results of these experiments were unexpected and suggest some aspects of potential molecular mechanisms of fibrinolysis, which will also be described here.

Fibrinogen Bastia (γ 318 Asp → Tyr) a Novel Abnormal Fibrinogen Characterized by Defective Fibrin Polymerization

1999 ◽  
Vol 82 (12) ◽  
pp. 1639-1643 ◽  
Author(s):  
Karim Chabane Lounes ◽  
Claudine Soria ◽  
Antoine Valognes ◽  
Marie France Turchini ◽  
Jaap Koopman ◽  
...  
Keyword(s):  
Calcium Ions ◽  
Clinical Symptoms ◽  
Degradation Products ◽  
Base Substitution ◽  
Chain Gene ◽  
Fibrinogen Concentration ◽  
Clotting Time ◽  
Terminal Part ◽  
Fibrin Polymerization ◽  
Chain Sequence

SummaryA new congenital dysfibrinogen, Fibrinogen Bastia, was discovered in a 20-year-old woman with no clinical symptoms. The plasma thrombin-clotting time was severely prolonged. The functional plasma fibrinogen concentration was low (0.2 mg/ml), whereas the immunological concentration was normal (2.9 mg/ml). Purified fibrinogen Bastia displayed a markedly prolonged thrombin-clotting time related to a delayed thrombin-induced fibrin polymerization. Both the thrombin-clotting time and the fibrin polymerization were partially corrected by the addition of calcium ions. The anomaly of fibrinogen Bastia was found to be located in the γ-chain since by SDS-PAGE performed according to the method of Laemmli two γ-chains were detected, one normal and one with an apparently lower molecular weight. Furthermore, analysis of plasmin degradation products demonstrated that calcium ions only partially protect fibrinogen Bastia γ-chain against plasmin digestion, suggesting that the anomaly is located in the C-terminal part of the γ-chain. Sequence analysis of PCR-amplified genomic DNA fragments of the propositus demonstrated a single base substitution (G → T) in the exon VIII of the γ chain gene, resulting in the amino acid substitution 318 Asp (GAC) → Tyr (TAC). The PCR clones were recloned and 50% of them contained the mutation, indicating that the patient was heterozygous. These data indicate that residue Asp 318 is important for normal fibrin polymerization and the protective effect of calcium ions against plasmin degradation of the C-terminal part of the γ-chain.

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