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Purification and characterization of a thermostable caseinolytic serine protease from the latex of Euphorbia heterophylla L.
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نویسنده
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singh s.j. ,singh l.r. ,devi s.k. ,singh s.s. ,devi c.b. ,rully h.
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منبع
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protein and peptide letters - 2015 - دوره : 22 - شماره : 9 - صفحه:828 -835
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چکیده
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A new thermostable caseinolytic serine protease was purified from the latex of euphorbia heterophylla l. to electrophoretic homogeneity by a procedure involving successive steps of pretreatment of the latex,peg fractionation,cm-cellulose chromatography and deae-cellulose chromatography. the purified protease was found to be a monomeric protein of molecular weight 77.2 kda. it exhibited caseinolytic activity with hyperbolic azocasein saturation with vmax and km values of 0.11 units.ml-1 and 0.55 mg.ml-1 respectively. specific inhibitory studies revealed the enzyme to be a serine protease. the protease was characterized by ph optimum of 8.0 and high thermostability with t1/2 of 75°c. based on the results of peptide mass fingerprinting analysis,the protease was shown to be a new protein not characterized earlier. © 2015 bentham science publishers.
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کلیدواژه
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Euphorbia heterophylla; Plant latex; Protease; Serine protease
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آدرس
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laboratory of protein biochemistry,biochemistry department,manipur university,canchipur, India, laboratory of protein biochemistry,biochemistry department,manipur university,canchipur, India, laboratory of protein biochemistry,biochemistry department,manipur university,canchipur, India, laboratory of protein biochemistry,biochemistry department,manipur university,canchipur, India, chemistry department,imphal college, India, laboratory of protein biochemistry,biochemistry department,manipur university,canchipur, India
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Authors
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