scholarly journals The Identification of Starch Phosphorylase in the Developing Mungbean (Vigna radiataL.)

2006 ◽  
Vol 54 (3) ◽  
pp. 986-986
Author(s):  
Yuan-Tih Ko ◽  
Jin-Yi Chang ◽  
Ya-Ting Lee ◽  
Yi-Hui Wu
Keyword(s):  
Starch Phosphorylase

Some metabolic responses of bush bean plants to a subherbicidal concentration of certain s-triazine compounds

1970 ◽  
Vol 48 (12) ◽  
pp. 2213-2217 ◽  
Author(s):  
B. Singh ◽  
D. K. Salunkhe
Keyword(s):  
Nitrate Reductase ◽  
Nitrate Reduction ◽  
Adenosine Triphosphatase ◽  
Acid Synthesis ◽  
Controlled Environment ◽  
Transaminase Activity ◽  
Starch Phosphorylase ◽  
Phaseolus Vulgaris L ◽  
Bean Plants ◽  
Bush Bean

A solution containing 0.5 p.p.m. of atrazine, simazine, igran, or GS-14254 with 0.2% triton-B 1956 was applied to the foliage of 11-day-old seedlings of bush beans, Phaseolus vulgaris L. cultivar Tender-green, growing on vermiculite in a controlled environment. The activities of nitrate reductase, glutamic-pyruvic transaminase, α-amylase, starch phosphorylase, and adenosine triphosphatase were determined 5,10, and 20 days after treatment. In general, the activity of each of the five enzymes was stimulated by the treatment. The results suggest that protein increase following the application of.s-triazines to bean plants may stem in part from an enhanced rate of amino acid formation resulting from the induced increment in nitrate reductase and transaminase activity. The application of these chemicals also creates a metabolic condition favorable for greater use of carbohydrates needed for nitrate reduction and protein synthesis, and as a source of organic acid synthesis.

scholarly journals Tracking interactions that stabilize the dimer structure of starch phosphorylase from Corynebacterium callunae

2003 ◽  
Vol 270 (10) ◽  
pp. 2126-2136 ◽  
Author(s):  
Richard Griessler ◽  
Alexandra Schwarz ◽  
Jan Mucha ◽  
Bernd Nidetzky
Keyword(s):  
Starch Phosphorylase ◽  
Dimer Structure ◽  
Corynebacterium Callunae

Pollen development in maize plants subjected to molybdenum deficiency

1979 ◽  
Vol 57 (18) ◽  
pp. 1946-1950 ◽  
Author(s):  
S. C. Agarwala ◽  
C. Chatterjee ◽  
P. N. Sharma ◽  
C. P. Sharma ◽  
N. Nautiyal
Keyword(s):  
Acid Phosphatase ◽  
Pollen Development ◽  
Pollen Grains ◽  
Starch Phosphorylase ◽  
Maize Plants ◽  
Male Flowers

A reduction in the size of tassels, male flowers, and anthers resulted from molybdenum deficiency in maize. In molybdenum-deficient plants, anthesis was suppressed or delayed and the anthers had fewer and smaller pollen grains that lacked dense cytoplasmic contents, appeared shrivelled, and had poor viability. Because of molybdenum deficiency, there was a decrease in the activity of starch phosphorylase in mature and freshly shed pollen grains and decreases in the activities of invertase and acid phosphatase at all the five stages at which pollen grains were assayed for the enzymes. The activities of catalase and peroxidase were increased by molybdenum deficiency at all five stages and that of ribonuclease at four out of the five stages of pollen development.

Starch phosphorylase: Role in starch metabolism and biotechnological applications

2009 ◽  
Vol 29 (3) ◽  
pp. 214-224 ◽  
Author(s):  
R.S. Rathore ◽  
Neha Garg ◽  
Sarika Garg ◽  
Anil Kumar
Keyword(s):  
Biotechnological Applications ◽  
Starch Metabolism ◽  
Starch Phosphorylase

The Identification of Starch Phosphorylase in the Developing Mungbean (Vigna radiataL.)

2005 ◽  
Vol 53 (14) ◽  
pp. 5708-5715 ◽  
Author(s):  
Yuan-Tih Ko ◽  
Jin-Yi Chang ◽  
Ya-Ting Lee ◽  
Yi-Hui Wu
Keyword(s):  
Starch Phosphorylase

scholarly journals Maturation and subcellular compartmentation of potato starch phosphorylase.

1989 ◽  
Vol 1 (5) ◽  
pp. 559-566 ◽  
Author(s):  
N Brisson ◽  
H Giroux ◽  
M Zollinger ◽  
A Camirand ◽  
C Simard
Keyword(s):  
Potato Starch ◽  
Starch Phosphorylase ◽  
Subcellular Compartmentation

scholarly journals Influence of Variable Manganese and Silicon on the Nutrition, Sugar Production, and Enzyme Activity of Immature Sugarcane

1969 ◽  
Vol 53 (1) ◽  
pp. 14-27
Author(s):  
G. Samuels ◽  
Alex G. Alexander
Keyword(s):  
Enzyme Activity ◽  
Solution Culture ◽  
Sugar Production ◽  
Sugarcane Variety ◽  
Starch Phosphorylase ◽  
Sugarcane Plant ◽  
Stunted Growth ◽  
Mn Content ◽  
Si Content ◽  
Marked Suppression

Sugarcane variety M. 336 was grown in solution culture for 3 months under 3 Mn levels (0, 10, and 100 p.p.m.) and 3 Si levels (0, 50, and 500 p.p.m.) to study the influence of various levels of Mn and Si on growth, nutrient composition, and enzyme and sugar activity. The uptake of Mn by the immature sugarcane plant was definitely suppressed by increasing Si levels in the nutrient medium. As the Mn content of the plant dropped Si content increased. However, the converse did not hold, for when the cane plant was faced with an excessive supply of Mn, it attempted to compensate by increasing its Si uptake. High-Si X high-Mn treatment severely stunted growth, but yielded the maximum sucrose values recorded. Leaf-protein content was highest with all plants at the high Si level, but meristem protein reflected a reverse response. The greatly retarded growth caused by high Si and high Mn was accompanied by marked suppression of both starch phosphorylase and the phosphatases. Polyphenol oxidase showed a greater sensitivity to variable Mn and Si than any other enzyme assayed. Possible roles of Mn and Si in the mechanisms of auxin and protein synthesis are discussed.

scholarly journals Sucrose-Enzyme Relationships in Immature Sugarcane Treated With Variable Molybdenum, Calcium, Iron, Boron, Lead, Trichloroacetic Acid, Beta-glycerophosphate, and Starch

1969 ◽  
Vol 49 (4) ◽  
pp. 443-461
Author(s):  
Alex G. Alexander
Keyword(s):  
Trichloroacetic Acid ◽  
Foliar Spray ◽  
Sand Culture ◽  
Acid Phosphatases ◽  
Starch Phosphorylase ◽  
High Iron ◽  
High Calcium ◽  
Calcium Iron

Variable levels of the elements molybdenum, calcium, iron, lead, and boron, as well as trichloroacetic acid, ß-glycerophosphate, and starch, were supplied to immature sugarcane grown in the greenhouse. Molybdenum, calcium, and iron were provided in factorial combination to plants in sand culture. Molybdenum, lead, and starch were applied as foliar sprays to a second group of plants grown in soil, and boron, ß-glycerophosphate, plus trichloroacetic acid were likewise applied to the foliage of plants grown in soil. The objectives of these experiments were to determine whether any of the applied materials could alter the action of specific enzymes, and, if so, whether significantly greater sucrose content would result. Leaf and meristem tissues were assayed for sugars, and for the enzymes amylase, invertase, acid phosphatases, starch phosphorylase, peroxidase, and polyphenol oxidase. Molybdenum significantly increased sucrose when applied as a foliar spray (80 p.p.m.), and as a nutrient in sand culture (1 p.p.m.). The molybdenum effect was retarded or reversed when either high calcium (9 p.p.m.) or high iron (6 p.p.m.) was supplied concurrently. Acid phosphatases and amylase were suppressed by high molybdenum, although these effects were greatly dependent upon calcium and iron supply. When applied as a foliar spray, molybdenum suppressed amylase and the phosphatase hydrolyzing glucose-1-phosphate, but not ATP-ase or ß-glycerophosphatase. Invertase was suppressed by high iron (6 p.p.m.) when molybdenum and calcium were low, but was stimulated when molybdenum was high. Lead, when applied to leaves at the rate of 50 p.p.m., caused moderate sucrose increases. Glucose-1-phosphate phosphatase was suppressed by lead in leaves and meristem, as was starch phosphorylase in the leaves. Foliar starch application failed to stimulate amylase, while ß-glycerophosphate failed to inhibit starch phosphorylase or to induce greater phosphatase activity. A number of enzyme responses were obtained which do not happen in vitro, and known in vitro effects did not always appear when specific materials were applied to living plants. Trichloroacetic acid, in particular, appeared to stimulate rather than inhibit enzyme action in vivo. This and other consequences of applying enzyme-regulating materials are discussed in detail.

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