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세포응집물질을 생산하는 Aspergillus sp. LAM 94-142의 특성 및 물질생산 조건
이동희,이노운,이현우 건국대학교 산업기술연구원 1996 건국기술연구논문지 Vol.21 No.-
토양에서 분리한 세포응집물질을 생산하는 균주 LAM 94-142는 형태, 배양 및 생리학적 특성을 조사한 결과 Aspergillus parasiticus 또는 그 근연균으로 동정되었으며 물질을 생산하기 위한 배양최적 조건을 검토한 결과는 다음과 같다. 최적 탄소원과 질소원은 각각 1.5% glucose와 0.35% yeast extract였으며 Ca²+을 첨가하였을 때 물질생산이 현저히 증가되었으며 K+, Cu²+, Fe²+ 등의 금속이온은 물질 생성을 저해하였다. 또 인산의 K염은 물질 생합성을 촉진하였으나 ammonium염은 크게 저해하였다. 그리고 최적 초발 pH와 온도는 pH7과 30℃였으며 4일간 배양하였을 때 물질 생산량이 최대였다. A strain of mold, LAM 94-142, capable of producing cell aggregation factor was isolated from soil and identified as Aspergillus parasiticus or its related strain on the morphological, cultural and physiological characteristics. For production of the cell aggregation factor, glucose and yeast extract was favorable as carbon and nitrogen source, respectively. The factor production was increased by the addition of Ca²+ and potassium phosphates but inhibited by K+, Cu²+, Fe²+ and ammonium phosphates. Optimal initial pH and temperature for the factor production was pH 7 and 30℃, respectively. The production of the factor reached at maximum after 4 days in the medium containing 1.5% glucose, 0.35% yeast extract, 0.07% CaCl₂, and 0.05% KH₂PO₄.
Mutant Recombinant Hemoglobin ( α96Val → Tyr ) Exhibits Low Oxygen Affinity and High Cooperativity
Lee, Hyean Woo,Choi, Jong Whan,Kim, Hyun Won,Han, Dong Pyou,Jung, Seun Ho,Yeh, Byung Il,Sohn, Joon Hyung 생화학분자생물학회 2000 BMB Reports Vol.31 No.6
To investigate conformational information of a low oxygen affinity recombinant hemoglobin (rHb) containing 96Val→Trp mutation at the α96 position, we have produced rHb (α96Val→Phe) and rHb (a96Val→Tyr), using the Escherichia coli expression system and site-directed mutagenesis. The oxygen affinity of rHb (α96Val→Phe) is similar to that of human normal adult hemoglobin (Hb A). However, the oxygen affinity of rHb (α96Val→Tyr) showed much lower oxygen affinity than Hb A which is similar to that of rHb (α96Val→Trp), providing an opportunity as a potential candidate for a hemoglobin-based blood substitute. Both rHb (α96Val→Phe) and rHb (α96Val→Tyr) showed high cooperativity in oxygen binding. tH-NMR spectroscopy shows that both rHb (α96Val→Phe) and rHb (α96Val→Tyr) have very similar tertiary structure around the heme pockets and quaternary structure in the α₁β₂ subunit interface compared to Hb A. The low oxygen affinity of rHb (α96Val→Tyr) has been suggested to be due to a hydrogen bond caused by an extra hydroxyl group not present in rHb (α96Val→Phe). However, investigation of the carbonmonoxy form of rHb (α96Val→Phe) and (α96Val→Tyr) in the presence of inositol hexaphosphate at low temperature suggests that low oxygen affinity of (α96Val→Tyr) may arise from a mechanism different to that of rHb (α96Val→Trp).
Lee, Hyean Woo,Choi, Jong Whan,Kim, Hyun Won,Han, Dong Pyou,Jung, Seun Ho,Yeh, Byung Il,Sohn, Joon Hyung 생화학분자생물학회 2000 BMB Reports Vol.31 No.6
X-ray crystallographic studies of the deoxy form of human adult hemoglobin (Hb A) have shown that β99Asp is hydrogen bonded to both α42Tyr and α97Asn in the α₁β₂ subunit interface, suggesting that the essential role of β99Asp is to stabilize the deoxy-Hb by creating the intersubunit hydrogen bond. In particular, for Hb Kempsey (β99Asp→Asn), molecular dynamics simulation indicated that a new hydrogen bond involving β99Asn can be induced by replacing α42Tyr with a strong hydrogen-bond acceptor such as Asp. Designed mutant recombinant (r) Hb (β99Asp→Asn, α42Tyr→Asp) have been produced in the Escherichia coli expression system and have shown that functional defects of Hb Kempsey could be compensated by the α42Tyr→Asp substitution. However, as the α42Tyr→Asp mutation has never been reported before, it is still possible that the functional properties of r Hb (β99Asp→Asn, α42Tyr→Asp) may be due to the mutation itself. Thus, it is required to producer Hb (α42Tyr→Asp) and r Hb Kempsey (β99Asp→Asn) as controls, and to compare their properties with those of r Hb (β99Asp→Asn, α42Tyr→Asp). r Hb (α42Tyr→Asp) could not be purified because it is an unstable hemoglobin which forms Heinz bodies. r Hb Kempsey (β99Asp→Asn) exhibits very high oxygen affinity and greatly reduced cooperativity. Thus, r Hb (β99Asp→Asn) and r Hb (α42Tyr→Asp) compensate each other.
화분크기 및 관수간격이 도깨비고비의 생육에 미치는 영향
이현숙(Lee, Hyean-Suk),이희경(Lee, Hee-Kyeang),유동림(Yoo, Dong-Lim),남춘우(Nam, Chun-Woo),류승열(Ryu, Seung-Yeol),서종택(Suh, Jong-Taek) 한국자원식물학회 2006 한국자원식물학회지 Vol.19 No.4
도깨비고비 분화생산시에는 화분이 클수록 초장이 크고 엽수도 많았으며 엽장과 엽폭도 크게 나타났다. 도깨비고비는 화분크기 및 저면 관수 주기 모두 통계적 유의성이 인정되어 직경 $7{\sim}10cm$ 수식 이미지크기의 화분은 5일에 한번씩 저면 관수하는 것이 좋은 것으로 나타났다. This experiment was carried out to find out proper pot size and bottom irrigation interval for the flowerpot cultivation of Cyrtomium falcatum, 3 different pot sizes (5, 7, 10cm in diameter) and 3 irrigation interval (1 day, 3 days, 5 days) were treated by completely randomized design with 3 replications. Growth characteristics of Cyrtomium falcatum were investigated every 30 days after planting. The pot size of 7 to 10cm in diameter and the irrigation interval of 5 days appeared to be appropriate for Cyrtomium falcatum cultivation.