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牛血红蛋白的差异。

Differences in cattle globins.

作者信息

Efremov G, Braend M

出版信息

Biochem J. 1965 Dec;97(3):867-9. doi: 10.1042/bj0970867.

Abstract
  1. Comparisons have been made between electrophoretic mobilities of the cattle haemoglobins, HbA, HbB, HbC, HbD and HbF, at pH8.9. The fastest was HbB, then came in decreasing order HbF, HbC, HbA and HbD. 2. Globins were prepared from the main fractions of the five haemoglobins by CM-cellulose chromatography and investigated by starch-gel electrophoresis in four different buffer systems. In three of these (pH2.0 and 11.8) the globins appeared as two bands on stained starch gels. The slowest bands, the alpha-chains, showed the same rate of migration in all five globins. The faster bands, the non-alpha-chains, differed, that of HbF being the fastest and that from HbC the slowest. The other three were intermediate with, however, very small difference between the non-alpha-chains from HbA and HbD. 3. At pH1.8 in an acetate-phosphate-hydrochloric acid-urea buffer three bands appeared in all five globins of which the two slowest were indistinguishable in rates of migration, whereas the rates of migration of the third and fastest bands differed. Explanations for the occurrence of three bands are discussed.
摘要
  1. 已对牛血红蛋白HbA、HbB、HbC、HbD和HbF在pH8.9时的电泳迁移率进行了比较。迁移速度最快的是HbB,其次依次是HbF、HbC、HbA和HbD。2. 通过CM - 纤维素色谱法从这五种血红蛋白的主要组分中制备球蛋白,并在四种不同的缓冲系统中用淀粉凝胶电泳进行研究。在其中三种缓冲系统(pH2.0和11.8)中,球蛋白在染色的淀粉凝胶上呈现为两条带。最慢的带,即α链,在所有五种球蛋白中的迁移速率相同。较快的带,即非α链,则有所不同,其中HbF的迁移速率最快,HbC的最慢。另外三种处于中间状态,不过HbA和HbD的非α链之间差异非常小。3. 在乙酸盐 - 磷酸盐 - 盐酸 - 尿素缓冲液(pH1.8)中,所有五种球蛋白都出现了三条带,其中两条最慢的带在迁移速率上无法区分,而第三条也是最快的带的迁移速率则不同。文中讨论了出现三条带的原因。
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/843e/1264770/57b476d5fdd6/biochemj00760-0275-a.jpg

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