Flotation performance of a de-slimed（-150＋53μm）Jordanian siliceous phosphate was evaluated in a batch laboratory flotation column 100 cm high and 5 cm inside diameter.The collector used during anionic flotation wa...Flotation performance of a de-slimed（-150＋53μm）Jordanian siliceous phosphate was evaluated in a batch laboratory flotation column 100 cm high and 5 cm inside diameter.The collector used during anionic flotation was sodium oleate while an amine acetate（AEROMINE 3100C）was used for cationic flotation.Flotation comparison at different collector dosage,superficial gas velocity,and frother concentration showed that the maximum difference in performance between cationic and anionic flotation was obtained with these flotation parameters：30×10^（-6）（mg/L）frother concentration,250 g/t collector concentration,and 3.4 cm/s superficial gas velocity.At these operating conditions amine （cationic）flotation gave 7%higher flotation recovery,a 6%cleaner concentrate grade,and was 6%more efficient at removing silica.展开更多
目的优化非分型流感嗜血杆菌Haps蛋白质片段的分离纯化方法。方法采用盐析、透析脱盐、超滤浓缩、弱阳离子交换柱Hitrap CM Sepharose Fast Flow层析纯化Haps蛋白,优化Haps蛋白质片段的洗脱条件,包括pH值和离子强度,测定各洗脱液样品在2...目的优化非分型流感嗜血杆菌Haps蛋白质片段的分离纯化方法。方法采用盐析、透析脱盐、超滤浓缩、弱阳离子交换柱Hitrap CM Sepharose Fast Flow层析纯化Haps蛋白,优化Haps蛋白质片段的洗脱条件,包括pH值和离子强度,测定各洗脱液样品在280nm波长处的光吸收值(D280),用折线图显示,SDS-PAGE电泳检测分布图中处于峰值的样品,观察目的蛋白条带的出现。结果弱阳离子交换柱Hitrap CM Sepharose Fast Flow层析纯化HapS蛋白,缓冲液1洗脱液的D280分布为基线,缓冲液2洗脱液的D280分布折线图中有峰值出现,但峰有拖尾,SDS-PAGE电泳检测该洗脱峰主要为低分子量的蛋白条带;五种不同离子强度的缓冲液3洗脱液在100mmol/LNaCl离子强度时,D280的分布折线图显示有较高洗脱峰出现,SDS-PAGE电泳检测该洗脱峰有较明显的110000D的目的条带,其余离子强度下均未见明显洗脱峰出现。结论Sepharose CM FF层析柱分离纯化HapS蛋白质片段时,不同pH值的缓冲液对目的蛋白的洗脱没有明显影响,而主要影响杂蛋白的洗脱;100mmol/LNaCl离子强度的缓冲液3洗脱液获得较好的洗脱效果。展开更多
基金done during the first author's Fulbright fellowship at the Center for Advanced Separation (CAST)/Virginia Technical Institute and State University-USA. Salah would like to thank all the people who work at CAST for their friendship and support during his stay in Blacksburg, VA.
文摘Flotation performance of a de-slimed（-150＋53μm）Jordanian siliceous phosphate was evaluated in a batch laboratory flotation column 100 cm high and 5 cm inside diameter.The collector used during anionic flotation was sodium oleate while an amine acetate（AEROMINE 3100C）was used for cationic flotation.Flotation comparison at different collector dosage,superficial gas velocity,and frother concentration showed that the maximum difference in performance between cationic and anionic flotation was obtained with these flotation parameters：30×10^（-6）（mg/L）frother concentration,250 g/t collector concentration,and 3.4 cm/s superficial gas velocity.At these operating conditions amine （cationic）flotation gave 7%higher flotation recovery,a 6%cleaner concentrate grade,and was 6%more efficient at removing silica.
文摘目的优化非分型流感嗜血杆菌Haps蛋白质片段的分离纯化方法。方法采用盐析、透析脱盐、超滤浓缩、弱阳离子交换柱Hitrap CM Sepharose Fast Flow层析纯化Haps蛋白,优化Haps蛋白质片段的洗脱条件,包括pH值和离子强度,测定各洗脱液样品在280nm波长处的光吸收值(D280),用折线图显示,SDS-PAGE电泳检测分布图中处于峰值的样品,观察目的蛋白条带的出现。结果弱阳离子交换柱Hitrap CM Sepharose Fast Flow层析纯化HapS蛋白,缓冲液1洗脱液的D280分布为基线,缓冲液2洗脱液的D280分布折线图中有峰值出现,但峰有拖尾,SDS-PAGE电泳检测该洗脱峰主要为低分子量的蛋白条带;五种不同离子强度的缓冲液3洗脱液在100mmol/LNaCl离子强度时,D280的分布折线图显示有较高洗脱峰出现,SDS-PAGE电泳检测该洗脱峰有较明显的110000D的目的条带,其余离子强度下均未见明显洗脱峰出现。结论Sepharose CM FF层析柱分离纯化HapS蛋白质片段时,不同pH值的缓冲液对目的蛋白的洗脱没有明显影响,而主要影响杂蛋白的洗脱;100mmol/LNaCl离子强度的缓冲液3洗脱液获得较好的洗脱效果。
