Improved method for virus structural polypeptide analysis on dissociating acrylamide gel.
نویسندگان
چکیده
[This corrects the article on p. 760 in vol. 22.].
منابع مشابه
Protein kinase and phosphoproteins of avian myeloblastosis virus.
A protein kinase associated with purified virions of avian myeloblastosis virus, BAI strain A, was highly purified by ion-exchange chromatography and gel filtration. On the basis of molecular sieving on Sephadex G-200, the enzyme protein appeared to have a molecular weight of about 50,000 to 60,000; disc gel electrophoresis in sodium dodecyl sulfate-acrylamide gels revealed the presence of at l...
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High-resolution two-dimensional polyacrylamide gel electrophoresis (2-D PAGE) has provided the means for detailed analysis of polypeptide constituents of whole cells or subcellular fractions from a wide range of sources. To date, for the most part 2-D PAGE has been utilized for analytical separations, following the method originally described by O'Farrell (1). Urea, reducing agent, and a nonion...
متن کاملAnalysis of the in vitro product of an RNA-dependent RNA polymerase isolated from influenza virus-infected cells.
The products synthesized in vitro by an RNA-dependent RNA polymerase isolated from influenza virus-infected BHK21-F cells were analyzed by velocity sedimentation, annealing techniques, and acrylamide-agarose gel electrophoresis. Approximately 50% of the RNA synthesized in vitro remains associated with the 50 to 70S ribonucleoprotein complex containing polymerase activity; the remainder of the R...
متن کاملStructural proteins of adenovirus-associated viruses.
The structural proteins of adenovirus-associated virus (AAV) types 1, 2, and 3 were analyzed by acrylamide gel electrophoresis. In each case, one major protein (C) and two minor proteins (A and B) were identified. Component C had an estimated molecular weight of 62,000 daltons, and the molecular weights of components A and B were found to be 87,000 and 73,000 daltons, respectively. Coelectropho...
متن کاملReisfeld R A & Small P A. Electrophoretic heterogeneity of polypeptide chains of specific antibodies. Science 152:1253-5, 1966
This paper indicates that heavy and light polypeptide chains isolated from different specific antibodies to haptens and immunoglobulin (lgG) of normal rabbits can be resolved into distinct, multiple components by acrylamide gel electrophoresis in the presence of urea. Although both types of polypeptide chains could be resolved into multiple components, this method failed to distinguish antibodi...
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ورودعنوان ژورنال:
- Applied microbiology
دوره 23 3 شماره
صفحات -
تاریخ انتشار 1971