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 language | English (US) |
|---|---|
| Pages (from-to) | 421-429 |
| Number of pages | 9 |
| Journal | BBA - Enzymology |
| Volume | 315 |
| Issue number | 2 |
| DOIs | |
| State | Published - Aug 16 1973 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Medicine(all)
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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 journal › Article
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TY - JOUR
T1 - Studies on myrosinases. II. Purification and characterization of a myrosinase from rapeseed (Brassica napus L.)
AU - Lönnerdal, Bo
AU - Janson, Jan Christer
PY - 1973/8/16
Y1 - 1973/8/16
N2 - 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.).
AB - 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.).
UR - http://www.scopus.com/inward/record.url?scp=0015798629&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0015798629&partnerID=8YFLogxK
U2 - 10.1016/0005-2744(73)90272-6
DO - 10.1016/0005-2744(73)90272-6
M3 - Article
AN - SCOPUS:0015798629
VL - 315
SP - 421
EP - 429
JO - BBA - Enzymology
JF - BBA - Enzymology
SN - 0005-2744
IS - 2
ER -