[Isolation and properties of a protein with molecular mass of 50 kDa from free cytoplasmic mRNP-particles of rabbit reticulocytes].
A method of purification and isolation of the major protein with molecular mass of 50 kDa from free cytoplasmic mRNP particles of rabbit reticulocytes is described. According to the SDS-gel electrophoresis data a degree of isolated protein purity in the preparation is 95%. An isoelectric point of 50 kDa protein is found to be within 9.5 units of pH. A great share of glycine (20%) is typical of p50 amino acid composition as well as for other proteins of mRNP-particles.
V
V
Mynykh
I
I
Maĭdebura
N
N
Korneeva
V
V
Evdokimova
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001798:Blood Proteins / Q000737:chemistry / Q000302:isolation & purification*; D003593:Cytoplasm / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D008970:Molecular Weight; D011817:Rabbits; D012156:Reticulocytes / Q000737:chemistry*; D012261:Ribonucleoproteins / Q000737:chemistry / Q000302:isolation & purification*
D000596:Amino Acids; D001798:Blood Proteins; D012261:Ribonucleoproteins
Vydelenie i svoĭstva belka s molekuliarnoĭ massoĭ 50kDa iz svobodnykh tsitoplazmaticheskikh mRNP-chastits retikulotsitov krolika.