Price K M, Littler W A, Cummins P
Cardiovasc Res. 1980 Oct;14(10):555-60. doi: 10.1093/cvr/14.10.555.
Myosin was isolated from the free right and left ventricular wall of normal adult human myocardium and purified until actin contamination was considered negligible as judged by sodium dodecyl sulphate polyacrylamide gel electrophoresis and adenosine triphosphatase assay in the presence of magnesium chloride. Ca2+ and K+ ethylenediaminetetra-acetic acid activated adenosine triphosphatase activities were determined in the presence of 3 mmol.litre-1 adenosine triphosphate. Myosin light chain subunits, VLC-1 and VLC-2, were analysed by polyacrylamide gel electrophoresis using: (i) sodium dodecyl sulphate at pH 7.0; (ii) 6 mol.litre-1 urea at pH 8.5; and (iii) isoelectric focusing in 9.2 mol.litre-1 urea over the pH range 4 to 6. No inherent differences in enzymic or physiochemical properties of the myosins from the human right and left ventricle were observed. Similar results were obtained in the baboon and dog.
从正常成年人心脏的游离右心室壁和左心室壁中分离出肌球蛋白，并进行纯化，直至通过十二烷基硫酸钠聚丙烯酰胺凝胶电泳和在氯化镁存在下的三磷酸腺苷酶测定判断肌动蛋白污染可忽略不计。在3 mmol·升⁻¹三磷酸腺苷存在的情况下，测定了Ca²⁺和K⁺乙二胺四乙酸激活的三磷酸腺苷酶活性。使用以下方法通过聚丙烯酰胺凝胶电泳分析肌球蛋白轻链亚基VLC-1和VLC-2：(i) pH 7.0的十二烷基硫酸钠；(ii) pH 8.5的6 mol·升⁻¹尿素；(iii) 在9.2 mol·升⁻¹尿素中于pH 4至6范围内进行等电聚焦。未观察到来自人类右心室和左心室的肌球蛋白在酶学或物理化学性质上的固有差异。在狒狒和狗身上也获得了类似的结果。
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