Purification and characterisation of an inhibitor of rubber biosynthesis from C-serum of Hevea brasiliensis latex

Faridah Yusof, . and Ward Malcolm A., . and Walker John M., . Purification and characterisation of an inhibitor of rubber biosynthesis from C-serum of Hevea brasiliensis latex. pp. 95-110. ISSN 1511-1768

A proteinaceous inhibitor of rubber biosynthesis was purified from the C-serum of Hevea brasiliensis latex. The protein inhibited the incorporation of isopentenyl diphosphate into rubber. Purification was achieved by employing three column chromatography methods: Sephadex G-150 gel-filtration DEAE-Cellulose ion exchange chromatography and Phenyl Sepharose CL-4B hydrophobia interaction chromatography. The inhibitor makes up 0.3 of the total protein in the C-serum solids and was shown to have a molecular weight of 43 700 Da by mass spectrometry. The protein was blocked at the N-terminal. Amino acid sequence of peptide fragments obtained from CNBr endoproteinase Lysine-C and trypsin digestions showed this protein to have regions of sequence similar to patatin a protein that constitutes approximately 40 of the total protein present in mature potato tubers (Solanum tuberosum). Investigations showed that like patatin the inhibitor has lipolytic acyl hydrolase (LAH) activity. Based on these observations it is thought that the inhibitory effect is due to the destruction by LAH of the integrity of the rubber particle membrane in which the biosynthetic enzymes are thought to be embedded.

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Abstract

A proteinaceous inhibitor of rubber biosynthesis was purified from the C-serum of Hevea brasiliensis latex. The protein inhibited the incorporation of isopentenyl diphosphate into rubber. Purification was achieved by employing three column chromatography methods: Sephadex G-150 gel-filtration DEAE-Cellulose ion exchange chromatography and Phenyl Sepharose CL-4B hydrophobia interaction chromatography. The inhibitor makes up 0.3 of the total protein in the C-serum solids and was shown to have a molecular weight of 43 700 Da by mass spectrometry. The protein was blocked at the N-terminal. Amino acid sequence of peptide fragments obtained from CNBr endoproteinase Lysine-C and trypsin digestions showed this protein to have regions of sequence similar to patatin a protein that constitutes approximately 40 of the total protein present in mature potato tubers (Solanum tuberosum). Investigations showed that like patatin the inhibitor has lipolytic acyl hydrolase (LAH) activity. Based on these observations it is thought that the inhibitory effect is due to the destruction by LAH of the integrity of the rubber particle membrane in which the biosynthetic enzymes are thought to be embedded.

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Item Type:	Article
AGROVOC Term:	Hevea brasiliensis
AGROVOC Term:	Latex
AGROVOC Term:	Rubber
AGROVOC Term:	Biosynthesis
AGROVOC Term:	Biochemistry
AGROVOC Term:	Purification
AGROVOC Term:	Centrifugation
AGROVOC Term:	Enzyme activity
AGROVOC Term:	Solanum tuberosum
AGROVOC Term:	Proteins
Depositing User:	Ms. Suzila Mohamad Kasim
Last Modified:	24 Apr 2025 06:28
URI:	http://webagris.upm.edu.my/id/eprint/23316

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