Journal article
ALLIINASE (ALLIIN LYASE) FROM GARLIC (ALLIIUM-SATIVUM) IS GLYCOSYLATED AT ASN(146) AND FORMS A COMPLEX WITH A GARLIC MANNOSE-SPECIFIC LECTIN
Glycoconjugate Journal, Vol.12(5), pp.690-698
Oct/1995
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 alpha-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 Asn(146) in the sequence ASn(146)-Met(147)-Thr(148).
Details
- Title
- ALLIINASE (ALLIIN LYASE) FROM GARLIC (ALLIIUM-SATIVUM) IS GLYCOSYLATED AT ASN(146) AND FORMS A COMPLEX WITH A GARLIC MANNOSE-SPECIFIC LECTIN
- Creators
- Aharon Rabinkov (null) - 972WIS_INST___113Meir Wilchek (null) - The Weizmann Institute of ScienceDavid Mirelman (null) - The Weizmann Institute of Science
- Resource Type
- Journal article
- Publication Details
- Glycoconjugate Journal, Vol.12(5), pp.690-698; Oct/1995
- Number of pages
- 9
- Language
- English
- DOI
- https://doi.org/10.1007/BF00731266
- Record Identifier
- 993262811603596
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