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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제27권 제1호
- 발행연도
- 2017.1
- 수록면
- 84 - 91 (8page)
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The concern over the use of melittin in honey bee venom due to its adverse reaction caused by allergens such as phospholipase A2 (PLA2) and hyaluronidase (HYA) has been an obstacle towards its usage. We developed a novel single-step method for melittin purification and the removal of PLA2 and HYA. This study explores the influence of pH, buffer compositions, salt concentration, and types of cation-exchange chromatography resins on the recovery of melittin and the removal of both HYA and PLA2. Melittin was readily purified with a strong cation-exchange resin at pH 6.0 with sodium phosphate buffer. It resulted in a recovery yield of melittin up to 93% (5.87 mg from a total of 6.32 mg of initial melittin in crude bee venom), which is higher than any previously reported studies on melittin purification. PLA2 (99%) and HYA (96%) were also successfully removed. Our study generates a single-step purification method for melittin with a high removal rate of PLA2 and HYA, enabling melittin to be fully utilized for its therapeutic purposes.
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참고문헌 (17)
참고문헌 신청
Cichocka-Jarosz E. / 2012 / Hymenoptera venom allergy in humans / Folia Med. Cracov 52 : 43 ~ 60
Corporation WB / / Worthington Enzyme manual
GE Healthcare / / Ion Exchange Chromatography and Chromatofocusing:Principles and Methods / GE Healthcare Handbooks
Hall T / 2015 / Alkaline cation-exchange chromatography for the reduction of aggregate and a mis-formed disulfide variant in a bispecific antibody purification process / J.
Maulet Y / 1982 / Purification from bee venom of melittin devoid of phospholipase A2contamination / Anal. Biochem 127 : 61 ~ 67
Corporation WB / / Worthington Enzyme manual
GE Healthcare / / Ion Exchange Chromatography and Chromatofocusing:Principles and Methods / GE Healthcare Handbooks
Hall T / 2015 / Alkaline cation-exchange chromatography for the reduction of aggregate and a mis-formed disulfide variant in a bispecific antibody purification process / J.
Maulet Y / 1982 / Purification from bee venom of melittin devoid of phospholipase A2contamination / Anal. Biochem 127 : 61 ~ 67
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