BASIC AND OTHER PROTEINS IN MICROSOMES OF RAT LIVER
- 1 August 1963
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 88 (2) , 206-212
- https://doi.org/10.1042/bj0880206
Abstract
Microsomes and preparations of ribonucleoprotein particles were extracted with O[degree]2N-HC1 and the amino acid composition of the proteins was determined. A portion of about 40% of the total protein could be extracted from purified ribosomes. The extracted proteins possessed 24% of basic and 18% of acidic amino acid residues. The principal_N-terminal groups found were alanine, proline, glycine and serine. There were marked differences in the proportions of alanine and glycine contained in the basic and the HC1 acid-insoluble proteins.Keywords
This publication has 16 references indexed in Scilit:
- Molecular weight of the protein from bovine liver ribosomesBiochemical and Biophysical Research Communications, 1962
- Further observations on the intracellular location and mechanism of action of liver enzymes catalysing the synthesis of l-ascorbic acidBiochemical Journal, 1962
- The presence of basic proteins in microsomesBiochimica et Biophysica Acta, 1960
- Factors which affect cold acclimatization.1960
- A stable ribonucleoprotein for amino acid incorporationBiochimica et Biophysica Acta, 1960
- Preparation and amino acid incorporating ability of ribonucleoprotein-particles from different tissues of the ratExperimental Cell Research, 1960
- The Amino Acid Composition of Proteins Isolated from the Ribonucleoprotein Particles of Rat LiverJournal of Biological Chemistry, 1959
- A study of the proteinase content and the chromatography of thymus histonesBiochemical Journal, 1959
- Fractionation of proteins of the microsomes of rat liver by means of a non-ionic detergentBiochemical Journal, 1958
- On the similarity of amino acid composition of microsomal nucleoprotein particlesArchives of Biochemistry and Biophysics, 1958