#TITLE_ALTERNATIVE#
The Latex of Hevea brasiliensis is a colloid system with rubber and non rubber components consisting of: protein, lipid, carbohydrate and others. It is believed that spesific protein present in latex play a role in latex flow. In this study hevamine one of the protein components, was isolated and pu...
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| Format: | Theses |
| Language: | Indonesia |
| Online Access: | https://digilib.itb.ac.id/gdl/view/9504 |
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| Institution: | Institut Teknologi Bandung |
| Language: | Indonesia |
| Summary: | The Latex of Hevea brasiliensis is a colloid system with rubber and non rubber components consisting of: protein, lipid, carbohydrate and others. It is believed that spesific protein present in latex play a role in latex flow. In this study hevamine one of the protein components, was isolated and purified from the bottom fraction of latex Hevea brasiliensis clones GT 1 and LCB. At every purification step the destabilization activity on a rubber suspension of the isolated hevamine fractions was investigated (Yip, 1968). Sedimentation fractionation in 65 % ammonium sulphate (FAS) showed that there is destabilization activity in the precipitate. FAS was then fractionized further on a column of Sephadex G 25 . This fractionation produced 2 fractions, FS-1 and FS-2. FS-1 showed destabilization activity whereas FS-2 did not show any activity. FS-1 was fractionated by CMC cation exchanges column chromatography. This fractionization produced two main fractions, FC-3 and FC-4, which both showed destabilization activity.<p>Characterization of FC-3 (Hevamin A) and FC-4 (Hevamin B) with polyacrylamide disc gel electrophoresis showed that both proteins are pure as indicated by the presence of one band on the electrophoregram. Using polyacrylamide SDS gel electrophoresis, both Hevamin A and Hevamin B, consist of one protein subunit with molecular weights of 30100 and 29400, respectively (for clone GT 1) whereas for clone LCB, the molecular weights for Hevamin are 29000 and 28600, respectively. Lysozyme activity determination (Tata et al., 1990) using E.Coli ATCC as a substrate showed activity values in units/mg of 430 and 580 for clone GT 1 and 380 and 610 for clone LCB for hevamin A and hevamin B, respectively. Quantitative analysis showed that Hevamin A and Hevamin B are present in higher amounts in clone LCB then in clone GT 1. Characterization of FC-3 (Hevamin A) and FC-4 (Hevamin B) with polyacrylamide disc gel electrophoresis |
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