Valyl‐tRNA, tryptophanyl‐tRNA, and seryl‐tRNA synthetases from yellow lupin seeds Lupinus luteus were purified to homogeneity by ammonium sulfate fractionation, hydrophobic chromatography on aminohexyl‐Sepharose column and affinity chromatography on tRNA‐Sepharose column. Valyl‐tRNA synthetase consists of one polypeptide chain of molecular weight 125000 as judged by Sephadex G‐200 gel filtration and dodecylsulfate‐polyacrylamide gel electrophoresis in the presence of reducing agent. Seryl‐tRNA synthetase, Mr= 110000, is composed of two 55000‐Mr subunits. Tryptophanyl‐tRNA synthetase exhibits molecular weight of 200000 on Sephadex G‐200 and 37000 in dodecylsulfate‐polyacrylamide gel electrophoresis. This indicates that tryptophanyl‐tRNA synthetase consists of several subunits (probably four). Since the seryl‐tRNA synthetase exhibits the same mobility on dodecylsulfate‐polyacrylamide gels both in the presence and absence of reducing agent it is concluded that there is no covalent bond(s) between the subunits of the enzyme. There is also no covalent bond(s) between the subunits of tryptophanyl‐tRNA synthetase.
|Original language||English (US)|
|Number of pages||10|
|Journal||European Journal of Biochemistry|
|State||Published - Jan 1 1975|
All Science Journal Classification (ASJC) codes