查詢結果分析
相關文獻
- Arylamine N-Acetyltransferase Activity in Staphylococcus Aureus
- Shikonin Inhibited Growth and N-acetylation of 2-aminofluorene in Bacteria Strains Staphylococcus aureus and Klebsiella pneumoniae
- Reduction in Staphylococcus Aureus Wound Colonization by Using Nasal Mupirocin in Burn Patients
- Pyomyositis in Childhood: A Case Report
- N-Acetyltransferase in Healthy Human Liver and Hepatoma Tissues
- 素食豆乾中金黃色葡萄球菌生長之模擬
- Effects of Vitamin E on Arylamine N-Acetyltransferase Activity in Klebsiella Pneumoniae
- Affect of Garlic Components Diallyl Sulfide and Diallyl Disulfide on Arylamine N-Acetyltransferase Activity in Rat Lymphocytes
- 金黃色葡萄球菌燙傷樣皮膚症候群(Staphylococcal Scalded-Skin Syndrome)
- Susceptibility Testing and Clinical Effect of Fusidic Acid in Oxacillin-Resistant Staphylococcus Aureus Infections
頁籤選單縮合
題 名 | Arylamine N-Acetyltransferase Activity in Staphylococcus Aureus=金黃色葡萄球菌發現含有乙醯轉移酵素 |
---|---|
作 者 | 張芳菁; 鍾景光; 張文正; 吳禮字; 陳光偉; 張世憲; | 書刊名 | 中華民國微生物及免疫學雜誌 |
卷 期 | 30:3 1997.08[民86.08] |
頁 次 | 頁170-181 |
分類號 | 414.83 |
關鍵詞 | 金黃色葡萄球菌; 乙醯轉移酵素; Staphylococcus aureus; N-acctyltransferase; P-aminobenzoic acid; 2-aminofluorene; |
語 文 | 英文(English) |
中文摘要 | 金黃色葡萄球菌經萃取後之萃取液利用p-aminobenzoic acid(PABA)及2-amino-fluorene (2-AF)當作受質分別反應,再經由高壓液相層析儀分析。證實含有N-乙醯轉移酵素的活性存在。由細菌經萃取後而得N-乙醯轉移酵素的活性,以PABA為受質酵素的催化力是0.46±0.002 nmole/min/mg protein。若以2-AF為受質酵素的催化力是0.67±0.04 nmole/min/mg protein。以PABA為受質共K□質為2.35±0.39 mM,V□為9.43±0.78nmole/min/mg protein。以2-AF為受質其K□質為2.85±0.65 mM,V□為7.51±0.86 nmole/min/mg protein。此酵素反應最適宜的pH為7.0,最適宜的反應溫度為37℃。此酵素亦受iodoacetamide的抑制,當iodoacetamide濃度增加時,其抑制作用亦增強。二價離子中的鋅、鈣及鐵離子具較強抑制此酵素的活性作用。金黃色葡萄球菌N-乙醯轉移酵素的分子量約44.9kDa。這是第一次證明金黃色葡萄球菌含有N-乙醯轉移酵素。 |
英文摘要 | N-Acetyltransferase (NAT) activities were determined by incubation of Staphylococcus aureus cytosols with p-aminobenzoic acid (PABA) or 2-aminofluorene (2-AF) followed by high pressure liquid chromatography assays. The NAT activities from S. aureus were found to be 0.67 ±0.04 nmol/min/mg protein for the acetylation of 2-AF and 0.46 ± 0.02 nmol/ min/mg protein for thc acetylation of PABA. Thc apparent K and V□ values obtained were 2.85 ±0.65 mM and 7.51 ±0.86 nmol/min/mg protein for 2-AF, and 2.35 ±0.39 mM and 9.43 ±0.78 nmol/mln/mg protein for PABA, respectively. The optimal pH value for the enzyme activity was 7.0 for both substrates tested. The optimal temperature for enzyme activity was 37℃ for both substrates. Thc NAT activity was inhibited by iodoacetamide at 0.25 mM and activity was reduced 50%. At 1.0 mM iodoacetamide activity was inhibited more than 90%. Among a series of divalent cations and salts. Zn□, Ca□, and Fe□, werc demonstrated to be the most potent inhibitors. The molecular weight of NAT from S. aureus was found to be 44.9 kDa. This report is the first demonstration of acetyl CoA: arylamine NAT activity in S. aureus. |
本系統中英文摘要資訊取自各篇刊載內容。