نتایج جستجو برای: pisum sativum

تعداد نتایج: 7773  

2012
S. A. Al-Sohaimy

Lectins are carbohydrate binding proteins expressed in plants, animals and microorganisms and have been used to probe the surface properties of a wide range of prokaryotic and eukaryotic cells. The implication of some lectin molecules in several physiological processes has been claimed. The aim of this work is to purify the lectin from Egyptian pea (Pisum sativum) seeds and study its biochemica...

2017
Runchana Rungruangmaitree Wannee Jiraungkoorskul

Pisum sativum (Family: Fabaceae), as known as green pea or garden pea, has long been important in diet due to its content of fiber, protein, starch, trace elements, and many phytochemical substances. It has been shown to possess antibacterial, antidiabetic, antifungal, anti-inflammatory, antihypercholesterolemia, and antioxidant activities and also shown anticancer property. Its nonnutritive bi...

2005
Judith Brook S. H. West

Sunmmary. Phosfon-S, a substance which inhibits stem elongation, alters nucleic acid metaboli,sm in Pisutm sativum Alaska. Methylated albumin kieselguhr (MAK) columns were used to fractionate 32P-labeled nucleic acids. Phosfon-S treatment of the plants resulted in a decrease in soluble RNA and an increase in ribo,somal RNA. Specific activities of the various nucleic acid fractions were lower as...

Journal: :Plant physiology 1978
E M Beyer

A technique is described for eliminating the antiethylene effects of the Ag(+) ion in the intact pea plant (Pisum sativum). The technique is based on the ability of the ethylene mimic, acetylene, to negate the antiethylene effect of Ag(+), presumably through salt formation, and subsequently to induce the ethylene response.

Journal: :Plant physiology 1975
R B Kachru L E Anderson

When intact pea (Pisum sativum L.) plants are illuminated, the glycolytic enzyme phosphofructokinase is inactivated. In crude extracts the enzyme is inhibited by dithiothreitol. It would seem that this cytoplasmic enzyme, like glucose-6-P dehydrogenase, is light-inactivated when the enzymes of photosynthetic carbon metabolism are light-activated.

2017
Alexey Afonin Anton Sulima Aleksandr Zhernakov Vladimir Zhukov

Rhizobium leguminosarum bv. viciae RCAM1026 is a strain first isolated in 1964 from nodules of "Ramensky 77" cultivar of garden pea (Pisum sativum L.) now routinely used as a model strain in inoculation experiments on pea. Assembly with SPAdes yielded 133 contigs longer then 200 bp (N50 = 202,321, GC% = 60.84). Resulting annotated genome is 7,248,686 bp encoding 6792 genes.

Journal: :The Biochemical journal 1987
Z Glatz J Kovár L Macholán P Pec

Diamine oxidase was prepared from pea (Pisum sativum) seedlings by a new purification procedure involving two h.p.l.c. steps. We studied the optical and electrochemical properties of the homogeneous enzyme and also analysed the hydrolysed protein by several methods. The data presented here suggest that the carbonyl cofactor of diamine oxidase is firmly bound pyrroloquinoline quinone.

Journal: :Plant physiology 1984
J M Kobriger T W Tibbitts M L Brenner

Pea (Pisum sativum L. cv Alsweet) plants were exposed to mixtures of ozone plus sulfur dioxide at different times of the day. Injury, evaluated either as necrosis or chlorophyll, was greatest at midday when stomatal conductance was greatest. Abscisic acid levels were similar over the day, and showed no relation to stomatal conductance.

Journal: :Plant physiology 1977
M Shaykh C Soliday P E Kolattukudy

Rabbit antibody to cutinase-I, isolated from Fusarium solani f. pisi, was conjugated to ferritin. With this ferritin-conjugated antibody it was shown that germinating spores of this fungus excreted cutinase during the penetration of the host pisum sativum. This result constitutes the most specific and strongest evidence for an enzymic penetration of a plant cuticle by a pathogen during infection.

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