A mushroom lectin from ascomycete Cordyceps militaris
- Authors
- Jung, Eui Cha; Kim, Ki Don; Bae, Chan Hyung; Kim, Ju Cheol; Kim, Dae Kyong; Kim, Ha Hyung
- Issue Date
- May-2007
- Publisher
- ELSEVIER SCIENCE BV
- Keywords
- ascomycete; mushroom; Corayceps militaris; lectin
- Citation
- BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, v.1770, no.5, pp 833 - 838
- Pages
- 6
- Journal Title
- BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
- Volume
- 1770
- Number
- 5
- Start Page
- 833
- End Page
- 838
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/24091
- DOI
- 10.1016/j.bbagen.2007.01.005
- ISSN
- 0304-4165
- 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.
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