Preliminary studies of acid protease and its inhibitor in latex of Hevea brasiliensis


Citation

Kamaruzaman Ampon, . and Maria Salleh, . Preliminary studies of acid protease and its inhibitor in latex of Hevea brasiliensis. pp. 415-418. ISSN 0126-6128

Abstract

Acid protease (EC 3.5.23-) is confined mainly to the bottom fraction of ultracentrifuged Hevea brasiliensis latex. The enzyme has an optimum activity at pH 3.5 and is strongly inhibited by the specific inhibitor pepstatin. This study reports for the first time the presence of a protein inhibitor of the enzyme in the C serum of Hevea latex.


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Abstract

Acid protease (EC 3.5.23-) is confined mainly to the bottom fraction of ultracentrifuged Hevea brasiliensis latex. The enzyme has an optimum activity at pH 3.5 and is strongly inhibited by the specific inhibitor pepstatin. This study reports for the first time the presence of a protein inhibitor of the enzyme in the C serum of Hevea latex.

Additional Metadata

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Item Type: Article
Additional Information: 3 graphs; 1 table; 16 ref. Summary (En Ms)
AGROVOC Term: HEVEA BRASILIENSIS
AGROVOC Term: PROTEASAS
AGROVOC Term: LATEX/ FRACCIONAMIENTO
AGROVOC Term: TECNICAS ANALITICAS
Depositing User: Ms. Norfaezah Khomsan
Last Modified: 24 Apr 2025 05:55
URI: http://webagris.upm.edu.my/id/eprint/20205

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