Purification and characterization of hydroxynitrile lyase from Hevea brasiliensis
Material type:
TextPublication details: Plant science 1996Description: 25-31Subject(s): Summary: Hydroxynitrile lyase from Hevea brasiliensis (HbHNL) was purified to apparent homogeneity. Purified HbHNL consists of non-covalently linked monomers of 30kDa. HbHNL exhibits a typical Michaelis-Menten kinetics with a Km of 115 mM and the enzyme activity is strongly inhibited by diisopropyl fluorophosphate and diethyl pyrocarbonate indicating a serine and histidine in the active site. HbHNL is serologically related to the HNL from Manohot esculenta but not to other HNLs.
| Item type | Current library | Vol info | Status | |
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Journals
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RRII Library Physiology | Volume 115, Issue 1 | Journals |
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Hydroxynitrile lyase from Hevea brasiliensis (HbHNL) was purified to apparent homogeneity. Purified HbHNL consists of non-covalently linked monomers of 30kDa. HbHNL exhibits a typical Michaelis-Menten kinetics with a Km of 115 mM and the enzyme activity is strongly inhibited by diisopropyl fluorophosphate and diethyl pyrocarbonate indicating a serine and histidine in the active site. HbHNL is serologically related to the HNL from Manohot esculenta but not to other HNLs.
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