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Involvement of Hevea Latex Organelle Membrane Proteins in the Rubber Biosynthesis Activity and Regulatory Function

  1. Dhirayos Wititsuwaannakul1,*,
  2. Atiya Rattanapittayaporn2,
  3. Tanetoshi Koyama3,
  4. Rapepun Wititsuwaannakul2

Article first published online: 23 MAR 2004

DOI: 10.1002/mabi.200300080

Issue

Macromolecular Bioscience

Macromolecular Bioscience

Special Issue: Highlights from the First IUPAC International Conference on Bio-based Polymers (ICBP 2003) in Saitama, Japan

Volume 4, Issue 3, pages 314–323, March 15, 2004

Additional Information

How to Cite

Wititsuwaannakul, D., Rattanapittayaporn, A., Koyama, T. and Wititsuwaannakul, R. (2004), Involvement of Hevea Latex Organelle Membrane Proteins in the Rubber Biosynthesis Activity and Regulatory Function. Macromol. Biosci., 4: 314–323. doi: 10.1002/mabi.200300080

Author Information

  1. 1

    Department of Biochemistry, Faculty of Science, Mahidol University, Rama 6 Road, Bangkok 10400, Thailand

  2. 2

    Department of Biochemistry, Faculty of Science, Prince of Songkla University, Hat-Yai, Songkla 90112, Thailand

  3. 3

    Institute of Multidisciplinary Research for Advanced Materials (IMRAM), Tohoku University, Sendai 980, Japan

*Department of Biochemistry, Faculty of Science, Mahidol University, Rama 6 Road, Bangkok 10400, Thailand. Fax: 662-248-0375

Publication History

  1. Issue published online: 23 MAR 2004
  2. Article first published online: 23 MAR 2004
  3. Manuscript Accepted: 27 NOV 2003
  4. Manuscript Received: 31 OCT 2003

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Keywords:

  • enzymes;
  • Hevea latex;
  • membranes;
  • micelles;
  • rubber biosynthesis

Abstract

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Summary: Centrifugation of fresh Hevea rubber latex yields three distinct fractions. The sediment bottom fraction (BF) content of membrane-bound organelles is ca. 20 vol.-% of latex. Prolonged storage or delayed use of fresh latex will result in disintegration and loss of the bottom fraction. This is due to the osmotically sensitive BF rupture and its membrane debris being tightly bound to the top rubber particles (RP) phase. The BF membrane was found to be highly active for rubber biosynthesis (RB), in contrast to previous reports that describe RB only occurring on the RP surface. It was clearly shown that washed BF membrane (WBM) was much more active than fresh RP for RB activity. WBM was highly activated by SDS for RB in a biphasic manner, but SDS strongly inhibited the RP. Probably WBM micelle formation resulted in a highly increased active surface area for RB. C55-PP (UPP) was a very active allylic for WBM in RB function, but inactive for RP. Serial acetone extraction of WBM proteins showed a distinct profile of the fractions with different RB activity. WBM isolated proteins suspended in 2% sodium dodecyl sulfate (SDS) with an RB activity equal to that of intact WBM was with the 20% acetone protein fraction. The 60 and 80% fractions were inactive. Combining the 20 with 80% fractions showed a complete inhibition of RB activity. Complete RB loss was also found when WBM was mixed with the 80% fraction, indicating that WBM has both an enzyme system and a factor for regulation of the RB activity in a well controlled metabolic function for the latex RB process.

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