Studies on myrosinases. II. Purification and characterization of a myrosinase from rapeseed (Brassica napus L.)

Bo Lönnerdal, Jan Christer Janson

Research output: Contribution to journalArticle

55 Citations (Scopus)

Abstract

Myrosinases (EC 3.2.3.1) are a group of isoenzymes present in Cruciferaes which catalyze the hydrolysis of glucosinolates. The myrosinases from rapeseed (Brassica napus L.) have been purified and the main component isolated and characterized. It is a glycoprotein with a molecular weight of 135 000 which consists of two peptide chains with a molecular weight of 65 000 and contains about 14% carbohydrate. It exists in 3 forms with different carbohydrate compositions and the isoelectric points are 4.96, 4.99 and 5.06, respectively. This work describes the isolation and physicochemical characterization and makes a comparison between the myrosinases from rapeseed and white mustard (Sinapis alba L.).

Original languageEnglish (US)
Pages (from-to)421-429
Number of pages9
JournalBBA - Enzymology
Volume315
Issue number2
DOIs
StatePublished - Aug 16 1973
Externally publishedYes

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Sinapis
Brassica napus
Brassica rapa
Molecular Weight
Carbohydrates
Glucosinolates
Isoelectric Point
Isoenzymes
Glycoproteins
Hydrolysis
Peptides
thioglucosidase

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Studies on myrosinases. II. Purification and characterization of a myrosinase from rapeseed (Brassica napus L.). / Lönnerdal, Bo; Janson, Jan Christer.

In: BBA - Enzymology, Vol. 315, No. 2, 16.08.1973, p. 421-429.

Research output: Contribution to journalArticle

Lönnerdal, Bo ; Janson, Jan Christer. / Studies on myrosinases. II. Purification and characterization of a myrosinase from rapeseed (Brassica napus L.). In: BBA - Enzymology. 1973 ; Vol. 315, No. 2. pp. 421-429.
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