2016
DOI: 10.5897/jabsd2015.0249
|View full text |Cite
|
Sign up to set email alerts
|

Anti-insect potential of a lectin from the tuber, Dioscorea mangenotiana towards Eldana saccharina (Lepidoptera: Pyralidae)

Abstract: A lectin was purified from the tuber, Dioscorea mangenotiana in this study. The lectin agglutinated erythrocytes from human and rabbit, and the activity was inhibited by glucose and N-acetyl-Dglucosamine with minimum inhibitory concentration (MIC) of 50 and 25 mM, respectively. The lectin was composed of two isoforms, DML I and DML II. The apparent native molecular mass of DML I was estimated at 51 kDa and the subunit molecular mass at 25 kDa, suggesting a dimeric structure. The lectin was stable up to 90°C an… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1

Citation Types

0
1
0

Year Published

2020
2020
2022
2022

Publication Types

Select...
4

Relationship

1
3

Authors

Journals

citations
Cited by 4 publications
(1 citation statement)
references
References 40 publications
0
1
0
Order By: Relevance
“…Lectins are a heterogeneous group of (glyco)proteins that bind reversibly and specifically to glyco-moieties with several biological properties such as insecticidal [1,2], antinociceptive, anti-inflammatory [3], antiviral [4], antifungal, antibacterial, antiproliferative [5,6], anthelmintic [7,8], and mitogenic [9] activities. The stability or biological activities of most of these proteins remain stable, even when subjected to harsh conditions, and are therefore considered strong candidates for therapeutic use [10].…”
Section: Introductionmentioning
confidence: 99%
“…Lectins are a heterogeneous group of (glyco)proteins that bind reversibly and specifically to glyco-moieties with several biological properties such as insecticidal [1,2], antinociceptive, anti-inflammatory [3], antiviral [4], antifungal, antibacterial, antiproliferative [5,6], anthelmintic [7,8], and mitogenic [9] activities. The stability or biological activities of most of these proteins remain stable, even when subjected to harsh conditions, and are therefore considered strong candidates for therapeutic use [10].…”
Section: Introductionmentioning
confidence: 99%