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Rubber Biosynthesis By Immature Rubber Particle (IRP)

Rubatex Msds       408 Faculty of Science RUBBER BIOSYNTHESIS BY IMMATURE RUBBER PARTICLE (IRP)

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Rubatex Neoprene Daranee Tong-in1, Dhirayos Wititsuwannakul1 and Rapepun Wititsuwannakul2 1Department of Biochemistry, Faculty of Science, Mahidl University, 2Department of Biochemistry, Faculty of Science, Prince of Songkhla University

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Rubatex Pipe Insulation Key words: rubber biosynthesis, rubber particle, Hevea brasiliensis

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Rubatex 180

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Rubatex 180 Fs                      Rubber biosysnthesis measured as incorporation of radiolabelled isoprene from 14C-isopentenyl pyrophospohate (IPP) into rubber molecule, was assayed in suspensions of immature rubber particle (IRP or Zone 2). The rubber transferase activity was characterized with respect to substrate and IRP concentration. The rate of 14C-IPP-incorporation was dependent upon the concentration of 14C-substrate and IRPs, incubation time, pH and temperature of incubation. Rubber biosynthesis of IRPs (Zone 2) was inhibited by lectin from latex lutoid membrane (l7 kD). Analysis of protein extraction of IRP by SDS-PAGE revealed a simple protein profile characteristic of Heves IRP, containing l4 and 24 kD.   STUDY OF PROTEASE INHIBITOR IN HEVEA LATEX Wannapa Sritanyarat, Dhirayos Wititsuwannakul1 and Rapepun Wititsuwannakul2 1Department of Biochemistry, Faculty of Science, Mahidl University, Bangkok l0400.,2Department of Biochemistry, Faculty of Science, Prince of Songkhla University, Hat-Yai 91002.

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Rubatex 320 Key words: protease inhibitor, Hevea brasiliensis, latex

Rubatex 373

                     Fresh latex was fractionated by ultracentrifugation at 49,000 x g for 45 min. into 3 distinct separated zones namely rubber, C-serum and bottom fraction. Protease inhibitor (PI) was detected in both C-serum and B-serum (from bottom) fractions. The C-serum PI was purified by scetone fractionation and obotained in 80-95% acetone (v/v) pellet fraction. The molecular weight of purified PI was about 6.5 kD under SDS-PAGE. The protein PI was found to be very heat stable. It could be boiled upto l40 min. with only about 40% lost of activity.

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