cotyledon orbiculata/protease

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Evidence for the probable oil body association of a thiol-protease, leading to oleosin degradation in sunflower seedling cotyledons.

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The activity of a 65 kDa, cytosolic protease from sunflower seedling cotyledons coincides with the degradation of oleosins during seed germination. Further investigations carried out in this laboratory have demonstrated the probable association of a thiol-protease with oil bodies, leading to gradual

Purification and characterization of cysteine protease from germinating cotyledons of horse gram.

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BACKGROUND Proteolytic enzymes play central role in the biochemical mechanism of germination and intricately involved in many aspects of plant physiology and development. To study the mechanism of protein mobilization, undertaken the task of purifying and characterizing proteases, which occur

Emergence of proteases in germinating cucumber cotyledons and their roles in the two-step degradation of storage protein.

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The degradation of storage protein in germinating cucumber seeds was shown to proceed via two distinct steps. First, several proteases with acidic isoelectric points (pIs) were involved in solubilization and partial degradation of 11S globulin. Treatment of seedlings with cycloheximide inhibited

Proteomic Investigations of Proteases Involved in Cotyledon Senescence: A Model to Explore the Genotypic Variability of Proteolysis Machinery Associated with Nitrogen Remobilization Efficiency during the Leaf Senescence of Oilseed Rape.

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Oilseed rape is characterized by a low nitrogen remobilization efficiency during leaf senescence, mainly due to a lack of proteolysis. Because cotyledons are subjected to senescence, it was hypothesized that contrasting protease activities between genotypes may be distinguishable early in the

Purification and characterization of cathepsin B-like cysteine protease from cotyledons of daikon radish, Raphanus sativus.

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Plant cathepsin B-like cysteine protease (CBCP) plays a role in disease resistance and in protein remobilization during germination. The ability of animal cathepsin B to function as a dipeptidyl carboxypeptidase has been attributed to the presence of a dihistidine (His110-His111) motif in the

Protein Breakdown and Formation of Protease in Attached and Detached Cotyledons of Phaseolus vulgaris L.

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In contrast to earlier reported results of similar experiments in peas, in which almost no increase in protease activity occurred in incubated detached cotyledons, we report here an increase in protease activity in both attached and detached bean cotyledons. Detached bean cotyledons showed

Control of the formation of amylases and proteases in the cotyledons of germinating peas.

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Protease activity increased in attached cotyledons of germinated peas (Pisum sativum L. cv. Alaska) as the stored proteins declined but did not increase in excised cotyledons incubated for the same length of time. Cotyledons of seeds germinated in the presence of a casein hydrolysate solution

Histochemical studies on protease formation in the cotyledons of germinating bean seeds.

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Protease formation in Phaseolus vulgaris L. cotyledons during seed germination was studied histochemically using a gelatin-film-substrate method. Protease activity can be detected by this method on the 5th day of germination, at approximately the same time that a rapid increase of activity was

Partial characterization of a protease inhibitor which inhibits the major endopeptidase present in the cotyledons of mung beans.

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Germination of mung beans (Phaseolus aureus, Roxb.) is accompanied by an increase in the activity of the endopeptidase involved in storage protein metabolism. Enzyme activity in the cotyledons increases 25-fold during the first 5 days of germination. The cotyledons also contain inhibitory activity

Contribution and limit of the model of perfused cotyledon to the study of placental transfer of drugs. Example of a protease inhibitor of HIV: nelfinavir.

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OBJECTIVE The perfused cotyledon model is a very useful method to study placental transfer of drugs. Here we studied placental transfer of the human immunodeficiency virus protease inhibitor nelfinavir using the non-recirculating dual human placental perfusion with a main goal to determining the

Characterization of novel cysteine proteases from germinating cotyledons of soybean [Glycine max (L.) Merrill].

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The enzymatic properties of novel cysteine proteases D3-alpha and beta which were purified from germinating soybean cotyledons were investigated. The enzyme activities were exhibited in the presence of a thiol reagent, such as 2-mercaptoethanol, and apparently inhibited by E-64, a cysteine protease

Enzymatic characterization of germination-specific cysteine protease-1 expressed transiently in cotyledons during the early phase of germination.

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Papain-like cysteine protease activity that shows a unique transient expression profile in cotyledons of daikon radish during germination was detected. The enzyme showed a distinct elution pattern on DEAE-cellulose compared with cathepsin B-like and Responsive to dessication-21 cysteine protease.

Synthesis of a protease in germinating cotton cotyledons catalzed by mRNA synthesized during embryogenesis.

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Placental transfer of darunavir in an ex vivo human cotyledon perfusion model.

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Placental transfer of the HIV protease inhibitor darunavir was investigated in 5 term human cotyledons perfused with darunavir (1,000 ng/ml) in the maternal to fetal direction. The mean (± the standard deviation [SD]) fetal transfer rate (FTR) (fetal/maternal concentration at steady state from 30 to

Maturation of catalase precursor proceeds to a different extent in glyoxysomes and leaf peroxisomes of pumpkin cotyledons.

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As an approach to study the mechanism of the microbody transition (glyoxysomes to leaf peroxisomes) in greening pumpkin cotyledons, catalase molecules were purified from the two different types of microbody and their structural properties were compared. The purified glyoxysomal catalase was found to

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