Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2001-12-4
pubmed:abstractText
A protein designated unguilin was isolated from seeds of the black-eyed pea (Vigna unguiculata). It possesses a molecular weight of 18 kDa and an N-terminal sequence resembling that of cyclophilins and the cyclophilin-like antifungal protein from mung beans, and was adsorbed on Affi-gel blue gel and CM-Sepharose. Unguilin exerted an antifungal effect toward fungi including Coprinus comatus, Mycosphaerella arachidicola, and Botrytis cinerea. In addition, unguilin was capable of inhibiting human immunodeficiency virus-1 reverse transcriptase and the glycohydrolases a- and beta-glucosidases which are involved in HIV infection. Unguilin was devoid of lectin and ribonuclease activities. It inhibited methyl-3H-thymidine uptake by mouse splenocytes and it weakly inhibited translation in a rabbit reticulocyte lysate system. Unguilin resembles mungin in some aspects, but differs from it in others.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0277-8033
pubmed:author
pubmed:issnType
Print
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
353-9
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Isolation of unguilin, a cyclophilin-like protein with anti-mitogenic, antiviral, and antifungal activities, from black-eyed pea.
pubmed:affiliation
Department of Biochemistry, Faculty of Medicine, The Chinese University of Hong Kong, Shatin.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't