Alliinase (alliin lyase) from garlic (Alliium sativum) is glycosylated at ASN146 and forms a complex with a garlic mannose-specific lectin |
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Authors: | Aaron Rabinkov Meir Wilchek and David Mirelman |
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Institution: | (1) Department of Membrane Research and Biophysics, The Weizmann Institute of Science, 76100 Rehovot, Israel |
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Abstract: | Alliinase (EC 4.4.1.4) catalyses the production of allicin (thio-2-propene-1-sulfinic acid S-allyl ester), a biologically active compound which is also responsible for the characteristic smell of garlic. It was demonstrated that alliinase which contains 5.5–6% of neutral sugars, gives clear PAS-staining, binds to Con A and can form a complex with garlic mannose-specific lectin (ASA). Evidence that the formation of such a complex is mediated by the interaction of the carbohydrate of the glycoprotein enzyme with the lectin was obtained from a radioligand assay which demonstrated the binding of alliinase to ASA and competitive inhibition of this binding by methyl -d-mannoside. ASA I was shown as the lectin mainly present in the complex with alliinase. The results of this study also demonstrate that alliinase is glycosylated at Asn146 in the sequence Asn146-Met147-Thr148.Abbreviations ASA
(Allium sativum agglutini). Garlic mannose specific lectin(s)
- PMSF
Phenyl methyl sulfonyl fluoride
- HPLC
High performance liquid chromatography
- SDS-PAGE
Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate
- PAS
Periodic acid-Schiff reagent stain
- CAPS
3-(cyclohexylamino)-1-propanesulfonic acid
- TFA
Trifluoracetic acid
- HEPES
N-2-HydroxyethylpiperazineN -2-ethanesulfonic acid
- Tricine
N-2-hydroxyl-1,1-bis(hydroxymethyl)]-ethyl glycine
- PVDF
poly(vinylene difluoride) |
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Keywords: | garlic alliinase lectin site of glycosylation |
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