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PHYSICOCHEMICAL PROPERTIES OF THE PROTEOLYTIC ENZYME FROM THE LATEX OF THE MILKWEED, ASCLEPIAS SPECIOSA TORR. SOME COMPARISONS WITH OTHER PROTEASES : II. KINETICS OF PROTEIN DIGESTION BY ASCLEPAIN.
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1. The kinetics of milk clotting by asclepain, the protease of Asclepias speciosa, were investigated. At higher concentrations of enzyme, the clotting time was inversely proportional to the enzyme concentration. 2. The digestion of casein and hemoglobin in 6.6 M urea by asclepain follows the second
PHYSICOCHEMICAL PROPERTIES OF THE PROTEOLYTIC ENZYME FROM THE LATEX OF THE MILKWEED, ASCLEPIAS SPECIOSA TORR. SOME COMPARISONS WITH OTHER PROTEASES : I. CHEMICAL PROPERTIES, ACTIVATION-INHIBITION, pH-ACTIVITY, AND TEMPERATURE-ACTIVITY CURVES.
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1. A study has been made of the properties of a hitherto unreported proteolytic enzyme from the latex of the milkweed, Asclepias speciosa. The new protease has been named asclepain by the authors. 2. The results of chemical, diffusion, and denaturation tests indicate that asclepain is a protein. 3.
Multiple forms of the asclepains. Cysteinyl proteases from milkweed.
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Two groups of asclepains (EC 3.4.22.7) isolated from the latex of Asclepias syriaca L. (milkweed) were each separated into five homogeneous enzymes. The members of each group are of similar amino acid composition, and leucine is the common N-terminal residue. Michaelis values are reported for each
Thrombin like activity of Asclepias curassavica L. latex: action of cysteine proteases.
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OBJECTIVE
To validate the scientific basis of plant latex to stop bleeding on fresh cuts. Cysteine protease(s) from Asclepias curassavica (Asclepiadaceae) plant latex was assessed for pro-coagulant and thrombin like activities.
METHODS
A waxy material from the latex of Asclepias curassavica latex
Biochemical analysis of a papain-like protease isolated from the latex of Asclepias curassavica L.
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Most of the species belonging to Asclepiadaceae family usually secrete an endogenous milk-like fluid in a network of laticifer cells in which sub-cellular organelles intensively synthesize proteins and secondary metabolites. A new papain-like endopeptidase (asclepain c-II) has been isolated and
Insights into the hydrolytic activity of Asclepias fruticosa L. protease.
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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
PHYSICOCHEMICAL PROPERTIES OF THE PROTEOLYTIC ENZYME FROM THE LATEX OF THE MILKWEED, ASCLEPIAS SPECIOSA TORR. SOME COMPARISONS WITH OTHER PROTEASES : III. KINETICS OF THE HEAT INACTIVATION OF PAPAIN, BROMELIN, AND ASCLEPAIN.
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1. The rates of heat inactivation of papain, bromelin, and asclepain were determined at several different temperatures. Papain was by far the most resistant to heat. 2. The destruction of papain at 75-83 degrees and bromelin at 55-70 degrees followed the course of a first order reaction, except that
Homologies of the N-terminal sequences of asclepains and papain.
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Sequences to residue 21 have been determined for the two asclepains, cysteinyl proteases isolated from milkweed (Asclepias syriaca L.). These were compared with the sequence for papain, and extensive homology was found.
Purification and biochemical characterization of asclepain c I from the latex of Asclepias curassavica L.
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In this work we report the isolation, purification and characterization of a new protease from latex of Asclepias curassavica L. Crude extract (CE) was obtained by gathering latex on 0.1 M citric-phosphate buffer with EDTA and cysteine with subsequent ultracentrifugation. Proteolytic assays were
Sequencing and characterization of asclepain f: the first cysteine peptidase cDNA cloned and expressed from Asclepias fruticosa latex.
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Asclepain f is a papain-like protease previously isolated and characterized from latex of Asclepias fruticosa. This enzyme is a member of the C1 family of cysteine proteases that are synthesized as preproenzymes. The enzyme belongs to the alpha + beta class of proteins, with two disulfide bridges
Characterization of papain-like isoenzymes from latex of Asclepias curassavica by molecular biology validated by proteomic approach.
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Latices from Asclepias spp are used in wound healing and the treatment of some digestive disorders. These pharmacological actions have been attributed to the presence of cysteine proteases in these milky latices. Asclepias curassavica (Asclepiadaceae), "scarlet milkweed" is a perennial subshrub
Induced responses to herbivory and jasmonate in three milkweed species.
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We studied constitutive and induced defensive traits (latex exudation, cardenolides, proteases, and C/N ratio) and resistance to monarch caterpillars (Danaus plexippus) in three closely related milkweed species (Asclepias angustifolia, A. barjoniifolia and A. fascicularis). All traits showed
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