TESAURO DE PLANTAS MEDICINALES - BILINGÜE

Morrenia brachystephana Griseb.

Nota de alcance

PARTE UTILIZADA= Used part: Raices, tallos, hojas. 

ACCIÓN FARMACOLÓGICA= Pharmacological action: Galactógeno . 

ZONA GEOGRÁFICA= Geografical zone: N. y Centro de Argentina. 

Nota de alcance

ÚLTIMOS AVANCES EN LA QUÍMICA Y ACTIVIDADES BACTERIOLÓGICAS EN LAS PLANTAS MEDICINALES= Medicinal plants, last advances on chemistry and bacteria activities on the medicinal herbs

1) The properties of morrenain b II, a proteinase isolated from the latex of Morrenia brachystephana, were compared with those of morrenain o II, a proteinase obtained from the latex of Morrenia odorata.  Both peptidases were purified to homogeneity by acetone pptn. followed by cation exchange chromatog.  The enzymes have pI values higher than 9.3 and similar mol. masses (close to 26 kDa) as detd. by SDS-PAGE.  They display max. proteolytic activity within an alk. pH range, and also exhibit esterolytic activity.  The N-terminal sequences of morrenain o II and morrenain b II show a high degree of homol. between each other and to other cysteine plant proteinases.

2) Partial characterization of the crude proteolytic exts. of five Asclepiadaceae species namely Araujia hortorum Fourn., Asclepias curassavica L., Funastrum clausum (Jacq.) Schlechter, Morrenia brachystephana Griseb. and Morrenia odorata (Hook. et Arn.) Lindley, and a comparison of these results and those from other Asclepiadaceae species are reported.  Addnl., the crude ext. from M. brachystephana was submitted to further purifn. and characterization.  The crude enzyme showed high proteolytic activity when assayed on casein in the presence of 12 mM cysteine but was strongly inhibited by very low concns. of sodium iodoacetate (0.01 mM) and mercuric chloride (0.1 mM) suggesting that the enzyme belongs to the cysteinyl-protease type.  Fractioned acetone pptn. followed by cation exchange chromatog. allowed the sepn. of two basic (pI > 9.3) proteolytically active fractions, both homogeneous by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and with similar mol. masses (25.5 and 26 kDa).


Nota bibliográfica

1) TOURSARKISSIAN, Martín. Plantas medicinales de Argentina : sus nombres botánicos, vulgares, usos y distribución geográfica . Buenos Aires : Hemisferio Sur, 1980, p.12.

2) CAVALLI, Sandra Vairo, et al Comparison of two cysteine endopeptidases from latexes of Morrenia brachystephana Griseb. and Morrenia odorata (Hook et Arn.) Lindley (Asclepiadaceae). Biological Chemistry. 2001, vol.382, nº5, p.879-883.
 
3) ARRIBERE, Maria Cecilia, et al. Comparison of Asclepiadaceae latex proteases and characterization of Morrenia brachystephana Griseb. cysteine peptidases. Phytochemical Analysis. 1998, vol.9, nº6, p.267-273.
 

Morrenia brachystephana Griseb.

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Fecha de creación
03-Ago-2007
Término aceptado
03-Ago-2007
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0
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0
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1
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3
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