Thiol: disulphide oxidoreductase in latex of Hevea brasiliensis


Citation

Shanmugam B., . and Muniandy S., . Thiol: disulphide oxidoreductase in latex of Hevea brasiliensis. pp. 184-189. ISSN 0127-7065

Abstract

Thiol: disulphide oxidoreductase is being described for the first time in the latex of Hevea brasiliensis. The enzyme can be located in both 20 000 g and 100 000 g supernatants and is stable at 25C for up to 12 h at pH 8.3. The optimum pH for the enzyme is 8.2 and it is stable between pH 6.0 and 9.0 for up to 24 h. It appears as a single peak by gel filtration and isoelectric focusing studies and has a molecular weight around 100 000 daltons with an isoelectric point of 4.5.


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Abstract

Thiol: disulphide oxidoreductase is being described for the first time in the latex of Hevea brasiliensis. The enzyme can be located in both 20 000 g and 100 000 g supernatants and is stable at 25C for up to 12 h at pH 8.3. The optimum pH for the enzyme is 8.2 and it is stable between pH 6.0 and 9.0 for up to 24 h. It appears as a single peak by gel filtration and isoelectric focusing studies and has a molecular weight around 100 000 daltons with an isoelectric point of 4.5.

Additional Metadata

[error in script]
Item Type: Article
AGROVOC Term: Hevea brasiliensis
AGROVOC Term: Latex
AGROVOC Term: Thiols
AGROVOC Term: Enzymes
AGROVOC Term: Crude protein
AGROVOC Term: Enzyme activity
AGROVOC Term: Isoelectric focusing
AGROVOC Term: Filtration
AGROVOC Term: Molecular weight
Geographical Term: Malaysia
Depositing User: Ms. Suzila Mohamad Kasim
Last Modified: 28 Apr 2025 05:14
URI: http://webagris.upm.edu.my/id/eprint/23559

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