Alan Lin

Proposed Uniform Nomenclature for Mammalian Ribosomal Proteins

SummaryThe numbering systems for mammalian ribosomal proteins used in several laboratories have been correlated and a proposal for a standard system is presented.

The molecular weights of rat liver ribosomal proteins determined by "three-dimensional" polyacrylamide gel electrophoresis.

SummaryThe molecular weights of the proteins of rat liver ribosomes were determined by “three-dimensional” polyacrylamide gel electrophoresis. The proteins of the 40S subunit ranged in mass from 10000 to 44000 daltons; the number average and weight average molecular weights were 25400 and 28400. The proteins of the 60S subunit ranged in mass from 10000 to 53700; the number average and weight average molecular weights were 28000 and 31500.

Micro-scale two-dimensional polyacrylamide gel electrophoresis of ribosomal proteins

SummaryA specially designed apparatus and conditions are described for the rapid analysis of ribosomal proteins by two-dimensional gel electrophoresis on a micro scale. The resolution of proteins in electropherograms is comparable to that obtained with other systems, but because of miniaturization, only 0.5 to 1 μg of each protein is required, and the entire procedure, including electrophoresis in both dimensions, and staining and destaining can be completed in 6 to 7 hours.

The stimulation of Escherichia coli stringent factor-dependent synthesis of guanosine 3′, 5′-polyphosphate [(p)ppGpp] by rat liver ribosomal proteins

SummaryThe effect of groups of proteins from rat liver ribosomes on the Escherichia coli stringent factor-catalyzed synthesis of (p)ppGpp was tested. Most groups were capable of supporting (p)ppGpp synthesis; the exceptions were A40, B140, B240 and B160 which contain proteins which are relatively less basic than those in the active groups. The capacity of 30 individual rat liver ribosomal proteins to activate stringent factor was assessed; most sustained the synthesis of (p)ppGpp. Proteins S12, S21, L12, P1, and P2 (which are acidic or relatively acid) had no activity; proteins S6, S8, and L3 were the most active: the others had moderate activity.