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牛心脏天冬氨酸氨基转移酶的纯化及一般性质

Purification and general properties of aspartate aminotransferase of ox heart.

作者信息

Marino G, Greco A M, Scardi V, Zito R

出版信息

Biochem J. 1966 Jun;99(3):589-94. doi: 10.1042/bj0990589.

Abstract
  1. A five-step procedure for preparing highly purified aspartate aminotransferase from ox heart is described. 2. The homogeneity of the pure enzyme was established by criteria such as ultracentrifugation and electrophoresis in starch gel and in polyacrylamide gel. 3. The pure enzyme has an isoelectric point of about pH5, and E(1%) (1cm.) 14.40 at 278mmu. 4. The molecular weight of the pure enzyme was determined as 96000 by sedimentation equilibrium. 5. The pH optimum for the pure enzyme was about 8. It was determined by a new assay technique. 6. A difference in the electrophoretic migration rate between the enzyme from ox heart and brain and the enzyme from pig heart and brain suggests a species specificity rather than an organ specificity. 7. A new effect of deionization on the visible-absorption spectrum of the enzyme was observed.
摘要
  1. 描述了从牛心制备高纯度天冬氨酸转氨酶的五步程序。2. 通过超速离心以及在淀粉凝胶和聚丙烯酰胺凝胶中进行电泳等标准确定了纯酶的均一性。3. 纯酶的等电点约为pH5,在278毫微米处的E(1%)(1厘米)为14.40。4. 通过沉降平衡测定纯酶的分子量为96000。5. 纯酶的最适pH约为8。这是通过一种新的测定技术确定的。6. 牛心和牛脑的酶与猪心和猪脑的酶在电泳迁移率上的差异表明是物种特异性而非器官特异性。7. 观察到去离子化对该酶可见吸收光谱的一种新效应。
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a6fe/1265045/84b0b155de66/biochemj00754-0086-a.jpg

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