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Particules ribonucleoproteiques 40 s des noyaux de foie de rat. Proprietes des proteines de ces particules
Author(s) -
Sarasin Alain
Publication year - 1969
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(69)80267-x
Subject(s) - chemistry , residue (chemistry) , isoelectric point , electrophoresis , ribonucleoprotein , isoelectric focusing , chromatography , biochemistry , rna , gene , enzyme
Rat liver 40 S ribonucleoprotein particles, which are different from ribosomal subparticles, were isolated and the protein moiety studied. Disc electrophoresis at pH 4.5 and 8.8 suggests that these particles have a relatively simple protein structure, the proteins having isoelectric points which are near neutrality or slightly acidic. The amino acid composition shows an acidic residue/basic residue ratio of 1/1.39 and an as yet unidentified ninhydrin‐positive compound which is probably specific to these 40 S particles.