calotropis/protease

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Crystal and molecular structure of the sulfhydryl protease calotropin DI at 3.2 A resolution.

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The three-dimensional structure of the sulfhydryl protease calotropin DI from the madar plant, Calotropis gigantea, has been determined at 3.2 A resolution using the multiple isomorphous replacement method with five heavy atom derivatives. A Fourier synthesis based on protein phases with a mean

Comparative study on plant latex proteases and their involvement in hemostasis: a special emphasis on clot inducing and dissolving properties.

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In the present study we compared the clot inducing and dissolving properties of Calotropis gigantea R. Br. (Asclepiadaceae), Synadenium grantii Hook. f. (Euphorbiaceae) and Wrightia tinctoria R. Br. (Apocynaceae) latex extracts. All the three latex extracts hydrolyzed casein, fibrinogen and crude

Exploring applications of procerain b, a novel protease from Calotropis procera, and characterization by N-terminal sequencing as well as peptide mass fingerprinting.

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Procerain B is a novel cysteine protease isolated from Calotropis procera by our group and published recently. We have further characterized the enzyme by N-terminal sequencing and peptide mass fingerprinting. Procerain B showed maximum sequence similarity (80%) with Asclepain. Moreover, the

Biotechnological potential of a cysteine protease (CpCP3) from Calotropis procera latex for cheesemaking.

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This article reports the characterization and evaluation of the biotechnological potential of a cysteine protease purified from Calotropis procera (CpCP3). This enzyme was highly stable to different metal ions and was able to hydrolyze κ-casein similarly to bovine chymosin. Atomic force microscopy

Procerain B, a cysteine protease from Calotropis procera, requires N-terminus pro-region for activity: cDNA cloning and expression with pro-sequence.

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We have previously reported isolation and characterization of a novel plant cysteine protease, Procerain B, from the latex of Calotropis procera. Our initial attempts for active recombinant Procerain B in Escherichiacoli expression system was not successful. The reason for inactive enzyme production

Hemostatic, milk clotting and blood stain removal potential of cysteine proteases from Calotropis gigantea (L.) R. Br. Latex.

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BACKGROUND Plant latex is a natural source of biologically active compounds and several hydrolytic enzymes responsible for their diverse health benefits. Recent past has witnessed substantial progress in understanding their supplementary industrial and pharmaceutical utility. Calotropis gigantea is

Procerain, a stable cysteine protease from the latex of Calotropis procera.

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A protease was purified to homogeneity from the latex of medicinal plant Calotropis procera (Family-Asclepiadaceae). The molecular mass and isoelectric point of the enzyme are 28.8 kDa and 9.32, respectively. Hydrolysis of azoalbumin by the enzyme was optimal in the range of pH 7.0-9.0 and

Cysteine Protease Profiles of the Medicinal Plant Calotropis procera R. Br. revealed by de novo transcriptome analysis.

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Calotropis procera R. Br., a traditional medicinal plant in India, is a promising source of commercial proteases, because the cysteine proteases from the plant exhibit high thermo-stability, broad pH optima, and plasma-clotting activity. Though several proteases such as Procerain, Procerain B,

Plant latex thrombin-like cysteine proteases alleviates bleeding by bypassing factor VIII in murine model.

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Hemostasis is a tightly regulated process which maintains a fluid state of blood within the vasculature and provides thrombotic response upon tissue injury. Various scientific studies have implicated the role of plant latex proteases in hemostasis using in vitro experiments. However, in vivo models

Cysteine proteases from the Asclepiadaceae plants latex exhibited thrombin and plasmin like activities.

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In the present study we evaluated the presence of cysteine protease from the latex of four plants Asclepias curassavica L., Calotropis gigantea R.Br., Pergularia extensa R.Br. and Cynanchum puciflorum R.Br. belongs to the family Asclepiadaceae. Cysteine proteases from these plants latex exhibited

Purification and properties of the protease of latex of madar plants (Calotropis gigantea).

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Anti-inflammatory latex proteins of the medicinal plant Calotropis procera: a promising alternative for oral mucositis treatment

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Objective and design: Oral mucositis (OM) is an intense inflammatory reaction progressing to tissue damage and ulceration. The medicinal uses of Calotropis procera are supported by anti-inflammatory capacity. PII-IAA, a highly homogenous cocktail of laticifer

Latex proteins from the plant Calotropis procera are partially digested upon in vitro enzymatic action and are not immunologically detected in fecal material.

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Soluble proteins from the latex of Calotropis procera (LP) were investigated in vitro and in vivo for digestibility as the latex has previously been shown to produce considerable toxic effects on animals. The latex is also an important biologically active compound that displays antiinflammatory and

Differences in the unfolding of procerain induced by pH, guanidine hydrochloride, urea, and temperature.

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The structural and functional aspects along with equilibrium unfolding of procerain, a cysteine protease from Calotropis procera, were studied in solution. The energetic parameters and conformational stability of procerain in different states were also estimated and interpreted. Procerain belongs to

cDNA cloning and molecular modeling of procerain B, a novel cysteine endopeptidase isolated from Calotropis procera.

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Procerain B, a novel cysteine protease (endopeptidase) isolated from Calotropis procera belongs to Asclepiadaceae family. Purification of the enzyme, biochemical characterization and potential applications are already published by our group. Here, we report cDNA cloning, complete amino acid

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