A mushroom lectin from ascomycete Cordyceps militaris
DC Field | Value | Language |
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dc.contributor.author | Jung, Eui Cha | - |
dc.contributor.author | Kim, Ki Don | - |
dc.contributor.author | Bae, Chan Hyung | - |
dc.contributor.author | Kim, Ju Cheol | - |
dc.contributor.author | Kim, Dae Kyong | - |
dc.contributor.author | Kim, Ha Hyung | - |
dc.date.available | 2019-05-30T06:33:35Z | - |
dc.date.issued | 2007-05 | - |
dc.identifier.issn | 0304-4165 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/24091 | - |
dc.description.abstract | A mushroom lectin has been purified from ascomycete Cordyceps militaris, which is one of the most popular mushrooms in eastern Asia used as a nutraceutical and in traditional Chinese medicine. This lectin, designated CML, exhibited hemagglutination activity in mouse and rat erythrocytes, but not in human ABO erythrocytes. SDS-PAGE of CML revealed a single band with a molecular mass of 31.0 kDa under both nonreducing and reducing conditions that was stained by silver nitrate, and a 31.4 kDa peak in a Superdex-200 HR get-filtration column. The hemagglutination activity was inhibited by sialoglycoproteins, but not in by mono- or disaccharides, asialoglycoproteins, or de-O-acetylated glycoprotein. The activity was maximal at pH 6.0-9.1 and at temperatures below 50 degrees C. Circular dichroism spectrum analysis revealed that CML comprises 27% alpha-helix, 12% beta-sheets, 29% beta-turns, and 32% random coils. lts binding specificity and secondary structure are similar to those of a fungal lectin from Arthrobotrys oligospora. However, the N-terminal amino acid sequence of CML differs greatly from those of other lectins. CML exhibits mitogenic activity against mouse splenocytes. (c) 2007 Elsevier B.V. All rights reserved. | - |
dc.format.extent | 6 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | ELSEVIER SCIENCE BV | - |
dc.title | A mushroom lectin from ascomycete Cordyceps militaris | - |
dc.type | Article | - |
dc.identifier.doi | 10.1016/j.bbagen.2007.01.005 | - |
dc.identifier.bibliographicCitation | BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, v.1770, no.5, pp 833 - 838 | - |
dc.description.isOpenAccess | N | - |
dc.identifier.wosid | 000245832500013 | - |
dc.identifier.scopusid | 2-s2.0-33947121216 | - |
dc.citation.endPage | 838 | - |
dc.citation.number | 5 | - |
dc.citation.startPage | 833 | - |
dc.citation.title | BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS | - |
dc.citation.volume | 1770 | - |
dc.type.docType | Article | - |
dc.publisher.location | 네델란드 | - |
dc.subject.keywordAuthor | ascomycete | - |
dc.subject.keywordAuthor | mushroom | - |
dc.subject.keywordAuthor | Corayceps militaris | - |
dc.subject.keywordAuthor | lectin | - |
dc.subject.keywordPlus | ACID-SPECIFIC LECTIN | - |
dc.subject.keywordPlus | CARBOHYDRATE-BINDING SPECIFICITY | - |
dc.subject.keywordPlus | TRICHOLOMA-MONGOLICUM | - |
dc.subject.keywordPlus | POLYPORUS-SQUAMOSUS | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | FRUITING BODIES | - |
dc.subject.keywordPlus | PURIFICATION | - |
dc.subject.keywordPlus | FUNGUS | - |
dc.subject.keywordPlus | EXPRESSION | - |
dc.subject.keywordPlus | PROTEINS | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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