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cucumis maderaspatanus/protease
Link salvestatakse lõikelauale
Leht 1 alates 31 tulemused
Mutator-like elements identified in melon, Arabidopsis and rice contain ULP1 protease domains.
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The transposon Mutator was first identified in maize, and is one of the most active mobile elements in plants. The Arabidopsis thaliana genome contains at least 200 Mutator-like elements (MULEs), which contain the Mutator-like transposase gene, and often additional genes. We have detected a novel
Protease from the sarcocarp of Trichosanthes bracteata.
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A protease has been purified from sarcocarp of Trichosanthes bracteata (Lam.) Voigt by four steps of chromatography. Its M(r) was estimated by SDS-PAGE to be ca 67,000. The optimum pH of the enzyme was 11 at 35 degrees using casein substrate. The enzyme was strongly inhibited by di-isopropyl
Cucumisin like protease from the sarcocarp of Benincasa hispida var. Ryukyu.
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A protease has been purified from the sarcocarp of Benincasa hispida (Thunb.) Cogn. var. Ryukyu by two steps of chromatography. Its M(r) was estimated by SDS-PAGE to be about 67,000. The enzyme was strongly inhibited by diisopropyl fluorophosphate, but not by EDTA and cysteine protease inhibitors.
Cucumisin-like protease from the latex of Euphorbia supina.
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A protease has been purified from the latex of Euphorbia supina Rafin by two steps of chromatography. The Mr was estimated by SDS-PAGE to be 80 kDa. Its activity was inhibited strongly by diisopropyl fluorophosphate, but not by EDTA, pepstatin, or cysteine protease inhibitors, indicating that the
Protease D from the sarcocarp of honeydew melon fruit.
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A serine protease was purified from commercially available honeydew melon fruit (Cucumis melo L. var. inodorus Naud) by five steps including CM-Sepharose CL-6B column chromatography. At the first CM-Sepharose CL-6B chromatography four active fractions appeared. No difference in enzymatic properties
Purification and Some Properties of a Protease from the Sarcocarp of Musk Melon Fruit.
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A protease has been purified from sarcocarp of musk melon, Cucumis melo ssp. melo var. reticulatus Naud. Earl's Favourite. The protease was mostly present in the placenta part of the fruit and next in the inside mesocarp. The molecular mass of the enzyme was estimated to be about 62kDa on SDS-PAGE.
Structural basis of cucumisin protease activity regulation by its propeptide.
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Cucumisin [EC 3.4.21.25], a subtilisin-like serine endopeptidase, was isolated from melon fruit, Cucumis melo L. Mature cucumisin (67 kDa, 621 residues) is produced by removal of the propeptide (10 kDa, 88 residues) from the cucumisin precursor by subsequence processing. It is reported that
Cucumisin, a serine protease from melon fruits, shares structural homology with subtilisin and is generated from a large precursor.
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Cucumisin is a thermostable alkaline serine protease that is found in the juice of melon fruits (Cucumis melo L.). We have determined the complete nucleotide sequence of a cucumisin cDNA (2,552 nucleotides) and deduced the corresponding amino acid sequence. The open reading frame of the cDNA
Substrate specificity of honeydew melon protease D, a plant serine endopeptidase.
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The substrate specificity of honeydew melon (Cucumis melo var. inodorus Naud) protease D was studied by the use of synthetic substrates and oligopeptides derived from a protein hydrolyzate. The hydrolysis rates of succinyl-(L-Ala)1-3-p-nitroanilide (Suc-(Ala)1-3-pNA) the hydrolysis rate
Purification and characterization of a serine protease from Cucumis trigonus Roxburghi.
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Kachri fruit, Cucumis trigonus Roxburghi, contains high protease activity and has been used as meat tenderizer in the Indian subcontinent. A 67 kDa serine protease from Kachri fruit was purified by DEAE-Sepharose and CM-Sepharose chromatography, whose optimum activity was at pH 11 and 70 degrees C.
Molecular cloning and expression of Cucumisin (Cuc m 1), a subtilisin-like protease of Cucumis melo in Escherichia coli.
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BACKGROUND
Oral allergy syndrome resulted from plant-derived foods is frequent among adults. Allergy to melon (cucumis melo) is one of the most frequent fruit allergies in Iran. Three different major allergens have been found in Cucumis melo that Cuc m 1 (cucumisin) has been identified as the major
Efficient DNA extraction from nail clippings using the protease solution from Cucumis melo.
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Owing to the increasing importance of genomic information, obtaining genomic DNA easily from biological specimens has become more and more important. This article proposes an efficient method for obtaining genomic DNA from nail clippings. Nail clippings can be easily obtained, are thermostable and
Exploring a new serine protease from Cucumis sativus L.
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Coagulation is an important physiological process in hemostasis which is activated by sequential action of proteases. This study aims to understand the involvement of aqueous fruit extract of Cucumis sativus L. (AqFEC) European burp less variety in blood coagulation cascade. AqFEC hydrolyzed casein
Tenderization of buffalo meat using plant proteases from Cucumis trigonus Roxb (Kachri) and Zingiber officinale roscoe (Ginger rhizome).
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This study was conducted to develop a method for improving tenderness and overall qualities of tough buffalo meat using plant proteolytic enzymes from Cucumis trigonus Roxb (Kachri) and Zingiber officinale roscoe (Ginger rhizome). Their tenderizing efficacy was compared with the most popular enzyme
Crystal structure of cucumisin, a subtilisin-like endoprotease from Cucumis melo L.
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Cucumisin is a plant serine protease, isolated as an extracellular glycoprotein from the melon fruit Cucumis melo L. var. Prince. Cucumisin is composed of multiple domain modules, including catalytic, protease-associated, and fibronectin-III-like domains. The crystal structure of cucumisin was
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