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ficus benghalensis/protease
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Seite 1 von 32 Ergebnisse
Benghalensin, a highly stable serine protease from the latex of medicinal plant Ficus benghalensis.
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A serine protease was purified to homogeneity from the latex of medicinal plant Ficus benghalensis by a single step procedure using anion exchange chromatography. The enzyme, named benghalensin, has a molecular mass of 47 kDa (MALDI-TOF and SDS-PAGE). The purified protein is a glycoprotein, and the
An unusual thermostable aspartic protease from the latex of Ficus racemosa (L.).
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The most extensively studied ficins have been isolated from the latex of Ficus glabrata and Ficus carica. However the proteases (ficins) from other species are less known. The purification and characterization of a protease from the latex of Ficus racemosa is reported. The enzyme purified to
Characterization of proteases activities in Ficus carica cultivars.
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In this study, we characterized protease activities of 23 Ficus carica cultivars. Extracts of fruit, branch, and leaf of Masui Dauphine, one of the most representative F. carica cultivars in Japan, exhibited gelatin-hydrolyzing activity, both in the absence and presence of a cysteine
Activation and inactivation of human factor X by proteases derived from Ficus carica.
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We investigated the effect of proteases derived from Ficus carica (common fig) on human blood coagulation. The milky sap (latex) of several Ficus (F.) species contain ficin, which is a mixture of proteases. Ficin derived from Ficus carica shortened the activated partial thromboplastin time and the
Identification, purification and characterization of a novel collagenolytic serine protease from fig (Ficus carica var. Brown Turkey) latex.
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A novel collagenolytic serine protease was identified and then purified (along with ficin) to apparent homogeneity from the latex of fig (Ficus carica, var. Brown Turkey) by two step chromatographic procedure using gel and covalent chromatography. The enzyme is a monomeric protein of molecular mass
A cysteine protease from the latex of Ficus benjamina has in vitro anthelmintic activity against Haemonchus contortus.
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Haemonchus contortus is a gastrointestinal nematode that is responsible for high mortality rates in ruminant herds. The resistance of nematodes to synthetic anthelmintics is widespread and requires a continuous search for new bioactive molecules, such as proteins. The objective of this study was to
Pharmacological properties of a protease from ficus hispiad linn.
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A sulphydryl plant protease present in the latex of Ficus hispida Linn affects hatematological values in mice. The isolated protease was found to increase clotting time and erythrocyte sedimentation rate while haemoglobin conten, RBC count and WBC count were decreased in a dose dependent manner.
A contradictory action of procoagulant ficin by a fibrinolytic serine protease from Egyptian Ficus carica latex
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Ficus carica is one of the most popular and edible plants. Its trees emanate latex of high medical importance. The well-studied procoagulant effect of ficin is a hallmark of this latex which protrudes an interesting question of how can the plant control this effect? In the present work, we
Crystallization and preliminary X-ray analysis of four cysteine proteases from Ficus carica latex.
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The latex of the common fig (Ficus carica) contains a mixture of at least five cysteine proteases commonly known as ficins (EC 3.4.22.3). Four of these proteases were purified to homogeneity and crystals were obtained in a variety of conditions. The four ficin (iso)forms appear in ten different
Drupin, a cysteine protease from Ficus drupacea latex accelerates excision wound healing in mice
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Wound healing is a tightly regulated physiological process that restores tissue integrity after injury. Plant latex proteases (PLPs) are considered an integral part in herbal wound care as it interferes at different phases of the wound healing process. Although many studies have reported the
Decolorization of crude latex by activated charcoal, purification and physico-chemical characterization of religiosin, a milk-clotting serine protease from the latex of Ficus religiosa.
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The crude latex of Ficus religiosa is decolorized by activated charcoal. Decolorization follows the Freundlich and Langmuir equations. A serine protease, named religiosin, has been purified to homogeneity from the decolorized latex using anion exchange chromatography. Religiosin is a glycoprotein
A cysteine protease isolated from the latex of Ficus microcarpa: purification and biochemical characterization.
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A plant protease named microcarpain was purified from the latex of Ficus microcarpa by acetonic (20-40 % saturation) precipitation, Sephadex G-75 filtration, and Mono Q-Sefinose FF chromatography. The protease was purified with a yield of 9.25 % and a purification factor of 8. The molecular weight
A novel milk-clotting cysteine protease from Ficus johannis: Purification and characterization.
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Due to the need for calf rennet alternatives, many attempts have been made to find new proteases. A novel cysteine protease with milk-clotting activity was purified from Ficus johannis by cation exchange chromatography. The protease was stable in various pH (3.0-10.5) with the optimum at 6.5 and
Optimization and characterization of alkaline protease and carboxymethyl-cellulase produced by Bacillus pumillus grown on Ficus nitida wastes.
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The potentiality of 23 bacterial isolates to produce alkaline protease and carboxymethyl-cellulase (CMCase) on Ficus nitida wastes was investigated. Bacillus pumillus ATCC7061 was selected as the most potent bacterial strain for the production of both enzymes. It was found that the optimum
Indications for and application of debricin ficus protease.
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