Wheat superoxide dismutase isoenzymes

D. S. Robinson; J. K. Donnelly; S. M. Lawlor; P. J. Frazier; N. W R Daniels

doi:10.1006/jcrs.1996.0009

Wheat superoxide dismutase isoenzymes

D. S. Robinson, J. K. Donnelly, S. M. Lawlor, P. J. Frazier, N. W R Daniels

Leeds Trinity University

Research output: Contribution to journal › Article › peer-review

7 Citations (Scopus)

Abstract

Evidence was obtained indicating that the superoxide dismutase (SOD) A and B isoenzymes of the wheat cultivar Tonic are of the Cu/ Zn type, whereas the SOD-C group are similar to manganese containing dismutases. Heat inactivation plots showed that the enzymic activity in crude extracts was relatively stable up to 50°C. The thermodynamic parameters enthalpy, ΔH#, free energy, ΔG#, and entropy, ΔS#, were estimated for the thermal inactivation of extracted SOD activity and a purified SOD-C isoenzyme. The SOD-C isoenzyme was purified extensively and shown to contain two closely related tetrametic isozymes (pI6·0 and 66·1) of M_r 80 000. A M_r of 20 000 has been calculated for the subunits. The N-terminal amino acid sequence of the purified SOD-C could be aligned with that of the Mn-SOD enzyme of maize and showed 57% homology.

Original language	English
Pages (from-to)	93-101
Number of pages	9
Journal	Journal of Cereal Science
Volume	23
Issue number	1
DOIs	https://doi.org/10.1006/jcrs.1996.0009
Publication status	Published - Jan 1996

Keywords

Cereals
Heat inactivation
Superoxide dismutase
Wheat

Access to Document

10.1006/jcrs.1996.0009

Cite this

@article{2a5f7b12d0324b8da4dfe0a03c9da1c2,

title = "Wheat superoxide dismutase isoenzymes",

abstract = "Evidence was obtained indicating that the superoxide dismutase (SOD) A and B isoenzymes of the wheat cultivar Tonic are of the Cu/ Zn type, whereas the SOD-C group are similar to manganese containing dismutases. Heat inactivation plots showed that the enzymic activity in crude extracts was relatively stable up to 50°C. The thermodynamic parameters enthalpy, ΔH#, free energy, ΔG#, and entropy, ΔS#, were estimated for the thermal inactivation of extracted SOD activity and a purified SOD-C isoenzyme. The SOD-C isoenzyme was purified extensively and shown to contain two closely related tetrametic isozymes (pI6·0 and 66·1) of Mr 80 000. A Mr of 20 000 has been calculated for the subunits. The N-terminal amino acid sequence of the purified SOD-C could be aligned with that of the Mn-SOD enzyme of maize and showed 57% homology.",

keywords = "Cereals, Heat inactivation, Superoxide dismutase, Wheat",

author = "Robinson, {D. S.} and Donnelly, {J. K.} and Lawlor, {S. M.} and Frazier, {P. J.} and Daniels, {N. W R}",

year = "1996",

month = jan,

doi = "10.1006/jcrs.1996.0009",

language = "English",

volume = "23",

pages = "93--101",

journal = "Journal of Cereal Science",

issn = "0733-5210",

publisher = "Academic Press Inc.",

number = "1",

}

TY - JOUR

T1 - Wheat superoxide dismutase isoenzymes

AU - Robinson, D. S.

AU - Donnelly, J. K.

AU - Lawlor, S. M.

AU - Frazier, P. J.

AU - Daniels, N. W R

PY - 1996/1

Y1 - 1996/1

N2 - Evidence was obtained indicating that the superoxide dismutase (SOD) A and B isoenzymes of the wheat cultivar Tonic are of the Cu/ Zn type, whereas the SOD-C group are similar to manganese containing dismutases. Heat inactivation plots showed that the enzymic activity in crude extracts was relatively stable up to 50°C. The thermodynamic parameters enthalpy, ΔH#, free energy, ΔG#, and entropy, ΔS#, were estimated for the thermal inactivation of extracted SOD activity and a purified SOD-C isoenzyme. The SOD-C isoenzyme was purified extensively and shown to contain two closely related tetrametic isozymes (pI6·0 and 66·1) of Mr 80 000. A Mr of 20 000 has been calculated for the subunits. The N-terminal amino acid sequence of the purified SOD-C could be aligned with that of the Mn-SOD enzyme of maize and showed 57% homology.

AB - Evidence was obtained indicating that the superoxide dismutase (SOD) A and B isoenzymes of the wheat cultivar Tonic are of the Cu/ Zn type, whereas the SOD-C group are similar to manganese containing dismutases. Heat inactivation plots showed that the enzymic activity in crude extracts was relatively stable up to 50°C. The thermodynamic parameters enthalpy, ΔH#, free energy, ΔG#, and entropy, ΔS#, were estimated for the thermal inactivation of extracted SOD activity and a purified SOD-C isoenzyme. The SOD-C isoenzyme was purified extensively and shown to contain two closely related tetrametic isozymes (pI6·0 and 66·1) of Mr 80 000. A Mr of 20 000 has been calculated for the subunits. The N-terminal amino acid sequence of the purified SOD-C could be aligned with that of the Mn-SOD enzyme of maize and showed 57% homology.

KW - Cereals

KW - Heat inactivation

KW - Superoxide dismutase

KW - Wheat

UR - http://www.scopus.com/inward/record.url?scp=0011209026&partnerID=8YFLogxK

U2 - 10.1006/jcrs.1996.0009

DO - 10.1006/jcrs.1996.0009

M3 - Article

AN - SCOPUS:0011209026

SN - 0733-5210

VL - 23

SP - 93

EP - 101

JO - Journal of Cereal Science

JF - Journal of Cereal Science

IS - 1

ER -

Wheat superoxide dismutase isoenzymes

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this