PMID: 41505Jan 1, 1979

Isolation of the structural proteins of western equine encephalitis virus by isoelectric focusing

Archives of Virology
K Hashimoto, B Simizu


Western equine encephalitis virus was disrupted with Triton X-100 and subjected to isoelectric focusing in a sucrose or urea gradient. The two envelope proteins, E1 and E2 were not well separated in a sucrose gradient, while the E1 and E2 proteins were distinguished as two major peaks which focused in a urea gradient at about pH 7.5 and 10, respectively. Isolated E1 protein refocused at pH 6.5 in a sucrose gradient isoelectric focusing column. When Western equine encephalitis virus was treated with Triton X-100 in 0.01 M phosphate buffer (pH6), hemagglutinating E1 protein was solubilized, which isoelectrofocused at pH 6.5. Purified nucleocapsids focused at pH 4 in a sucrose gradient on an isoelectric focusing column. After ribonuclease treatment of the purified nucleocapsid more than 95 per cent of the viral RNA was acid-soluble, and hte nucleocapsid protein isoelectrofocused at about pH 4.


Mar 1, 1977·Infection and Immunity·J SymingtonM J Schlesinger
Jun 17, 1976·Biochimica Et Biophysica Acta·A HeleniusK Simons
May 11, 1973·Biochimica Et Biophysica Acta·A Helenius, H Söderlund
Feb 1, 1972·Virology·M J SchlesingerB W Burge
Mar 12, 1970·Biochemical and Biophysical Research Communications·K Simons, L Kääriäinen
Jun 1, 1970·Journal of Virology·N H Acheson, I Tamm
Sep 1, 1958·The American Journal of Tropical Medicine and Hygiene·D H CLARKE, J CASALS

Related Concepts

Phosphate buffers
Hemagglutinins, Viral
Viral Proteins
Encephalitis Virus, Western Equine
Nucleocapsid Proteins
Urea Measurement
Viral Nucleocapsid Location
Isoelectric Focusing

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