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Cloning,expression,purification,and quantification of the 17% N-terminal domain of apolipoprotein b-100 [Apolipoprotein B-100' ün %17 N-Terminal bölgesinin klonlanmasi,anlatimi,saflaştirilmasi ve kantifikasyonu]
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نویسنده
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khachfe h.m. ,atkinson d.
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منبع
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journal of cell and molecular biology - 2011 - دوره : 9 - شماره : 2 - صفحه:37 -42
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چکیده
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Apolipoprotein b-100 (apo b) is the sole protein component of normal human low density lipoprotein (ldl). elevated levels of ldl have been correlated with atherosclerosis and other coronary artery diseases. the large size of apo b (4536 aa) necessitates that it be studied in pieces corresponding to its structurally organized domains. the 17% n-terminal domain of apo b,simply b17,poses as one of these domains,having very specific structural characteristics. the current report describes a set of protocols for the cloning,expression,purification,and quantification of this important part of the protein.
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کلیدواژه
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Apolipoprotein (Apo B); C127 cells; Cloning; Low-density lipoprotein; Sf9 cells
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آدرس
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faculty of sciences-v,lebanese university,nabatieh,lebanon,departments of biological and biomedical sciences,lebanese international university,beirut,lebanon,department of physiology and biophysics and center for advanced biomedical research,boston university school of medicine,715 albany street, United States, department of physiology and biophysics and center for advanced biomedical research,boston university school of medicine,715 albany street, United States
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Authors
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