Partial characterization of the galactinol forming enzyme from leaves of cucumis sativus L.

D. M. Pharr, H. N. Sox, R. D. Locy, Steven C Huber

Research output: Contribution to journalArticle

Abstract

Uridine diphosphate-D-galactose: inositol galactosyltransferase, the enzyme responsible for galactinol synthesis, was purified 41-fold from leaves of Cucumis sativus L. by a combination of gel filtration and ion exchange chromatography. Mn2+ concentration influenced the pH optimum of the enzyme. At low Mn2+ concentration (0.2 mM) the optimum was at pH 7.0. At high Mn2+ concentration (7.0 mM) the optimum was pH 5.5. The enzyme was not found in lysates of chloroplasts isolated from cucumber leaves.

Original languageEnglish (US)
Pages (from-to)25-33
Number of pages9
JournalPlant Science Letters
Volume23
Issue number1
DOIs
StatePublished - Oct 1981

Fingerprint

Cucumis sativus
Enzymes
enzymes
uridine diphosphate
Uridine Diphosphate Galactose
galactosyltransferases
Galactosyltransferases
leaves
Ion Exchange Chromatography
Inositol
Chloroplasts
ion exchange chromatography
Galactose
galactose
cucumbers
Gel Chromatography
chloroplasts
gels
synthesis
6 beta-galactinol

Cite this

Partial characterization of the galactinol forming enzyme from leaves of cucumis sativus L. / Pharr, D. M.; Sox, H. N.; Locy, R. D.; Huber, Steven C.

In: Plant Science Letters, Vol. 23, No. 1, 10.1981, p. 25-33.

Research output: Contribution to journalArticle

Pharr, D. M. ; Sox, H. N. ; Locy, R. D. ; Huber, Steven C. / Partial characterization of the galactinol forming enzyme from leaves of cucumis sativus L. In: Plant Science Letters. 1981 ; Vol. 23, No. 1. pp. 25-33.
@article{870856e9c5c34bbe81921c5c8dc437a2,
title = "Partial characterization of the galactinol forming enzyme from leaves of cucumis sativus L.",
abstract = "Uridine diphosphate-D-galactose: inositol galactosyltransferase, the enzyme responsible for galactinol synthesis, was purified 41-fold from leaves of Cucumis sativus L. by a combination of gel filtration and ion exchange chromatography. Mn2+ concentration influenced the pH optimum of the enzyme. At low Mn2+ concentration (0.2 mM) the optimum was at pH 7.0. At high Mn2+ concentration (7.0 mM) the optimum was pH 5.5. The enzyme was not found in lysates of chloroplasts isolated from cucumber leaves.",
author = "Pharr, {D. M.} and Sox, {H. N.} and Locy, {R. D.} and Huber, {Steven C}",
year = "1981",
month = "10",
doi = "10.1016/0304-4211(81)90021-3",
language = "English (US)",
volume = "23",
pages = "25--33",
journal = "Plant Science",
issn = "0168-9452",
publisher = "Elsevier Ireland Ltd",
number = "1",

}

TY - JOUR

T1 - Partial characterization of the galactinol forming enzyme from leaves of cucumis sativus L.

AU - Pharr, D. M.

AU - Sox, H. N.

AU - Locy, R. D.

AU - Huber, Steven C

PY - 1981/10

Y1 - 1981/10

N2 - Uridine diphosphate-D-galactose: inositol galactosyltransferase, the enzyme responsible for galactinol synthesis, was purified 41-fold from leaves of Cucumis sativus L. by a combination of gel filtration and ion exchange chromatography. Mn2+ concentration influenced the pH optimum of the enzyme. At low Mn2+ concentration (0.2 mM) the optimum was at pH 7.0. At high Mn2+ concentration (7.0 mM) the optimum was pH 5.5. The enzyme was not found in lysates of chloroplasts isolated from cucumber leaves.

AB - Uridine diphosphate-D-galactose: inositol galactosyltransferase, the enzyme responsible for galactinol synthesis, was purified 41-fold from leaves of Cucumis sativus L. by a combination of gel filtration and ion exchange chromatography. Mn2+ concentration influenced the pH optimum of the enzyme. At low Mn2+ concentration (0.2 mM) the optimum was at pH 7.0. At high Mn2+ concentration (7.0 mM) the optimum was pH 5.5. The enzyme was not found in lysates of chloroplasts isolated from cucumber leaves.

UR - http://www.scopus.com/inward/record.url?scp=0342690544&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0342690544&partnerID=8YFLogxK

U2 - 10.1016/0304-4211(81)90021-3

DO - 10.1016/0304-4211(81)90021-3

M3 - Article

AN - SCOPUS:0342690544

VL - 23

SP - 25

EP - 33

JO - Plant Science

JF - Plant Science

SN - 0168-9452

IS - 1

ER -