TAILIEUCHUNG - Báo cáo khoa học: Purification and structural analysis of the novel glycoprotein allergen Cyn d 24, a pathogenesis-related protein PR-1, from Bermuda grass pollen

Bermuda grass pollen (BGP) contains a very complex mixture of allergens, but only a few have been characterized. One of the allergens, with an apparent molecular mass of 21 kDa, has been shown to bind serum IgE from 29% of patients with BGP allergy. A combination of chromato-graphic techniques (ion exchange and reverse phase HPLC) was used to purify the 21 kDa allergen. | iFEBS Journal Purification and structural analysis of the novel glycoprotein allergen Cyn d 24 a pathogenesis-related protein PR-1 from Bermuda grass pollen Lu-Ping Chow1 5 Li-Li Chiu1 Kay-Hooi Khoo2 Ho-Jen Peng3 Sue-Yee Yang3 Shih-Wen Huang4 and Song-Nan Su3 1 Graduate Institute of Biochemistry and Molecular Biology College of Medicine NationalTaiwan University Taipei Taiwan 2 Institute of Biochemistry Academia Sinica Taipei Taiwan 3 Department of MedicalResearch and Education Veterans GeneralHospital-Taipei Taipei Taiwan 4 Department of Pediatric Division of Immunology and Allergy University of Florida Gainesville FL USA 5 Department of MedicalGenetics NationalTaiwan University Hospital Taipei Taiwan Keywords allergen Bermuda grass pollen glycoprotein pathogenesis-related proteins purification Correspondence . Su Department of MedicalResearch and Education Taipei Veterans General Hospital Taipei Taiwan 112 Fax 886 22875 1562 Tel 886 22871 2121 ext. 3379 E-mail snsu@ Received 9 June 2005 revised 27 September 2005 accepted 3 October 2005 doi Bermuda grass pollen BGP contains a very complex mixture of allergens but only a few have been characterized. One of the allergens with an apparent molecular mass of 21 kDa has been shown to bind serum IgE from 29 of patients with BGP allergy. A combination of chromatographic techniques ion exchange and reverse phase HPLC was used to purify the 21 kDa allergen. Immunoblotting was performed to investigate its IgE binding and lectin-binding activities and the Lysyl-C endopeptidase digested peptides were determined by N-terminal sequencing. The cDNA sequence was analyzed by RACE PCR-based cloning. The protein mass and the putative glycan structure were further elucidated using MALDI-TOF mass spectrometry. The purified 21 kDa allergen was designated Cyn d 24 according to the protocol of International Union of Immunological Societies IUIS . It has a molecular mass of 18 411 Da by .

• Báo cáo khoa học
• Report medicine
• traditional medicine
• scientific reports
• tumor cells
• medical knowledge
• chemical reaction
• medical research
• analysis of cytoplasmic
• oxidation
• Crystal structure
• bacteria
• hemoglobin
• medicine
• cell proliferation
• breast cancer
• gastric cancer
• hormone medicine
• biochemical studies
• environmental medicine