Rowett Research Institute

About: Rowett Research Institute is a based out in . It is known for research contribution in the topics: Rumen & Population. The organization has 2986 authors who have published 4459 publications receiving 239472 citations.

Sample size and replication in 2D gel electrophoresis studies.

Abstract: Two-dimensional gel electrophoresis can be an expensive technology, and many studies are based on a modest number of replicates. It is important that the statistical power is sufficient to detect protein expression differences of interest. This paper reviews the application of power calculations and considers how other issues affect the choice of sample size. The important distinction between biological and technical replication is made, and the superiority of the former is emphasized.

Hydrolysis of 14C-labelled proteins by rumen micro-organisms and by proteolytic enzymes prepared from rumen bacteria

Abstract: Proteins were labelled with 14C in a limited reductive methylation using [14C]formaldehyde and sodium borohydride. The rate of hydrolysis of purified proteins was little (less than 10%) affected by methylation and the 14C-labelled digestion products were not incorporated into microbial protein during a 5 h incubation with rumen fluid in vitro. It was therefore concluded that proteins labelled with 14C in this way are valid substrates for study with rumen micro-organisms. The patterns of digestion of 14C-labelled fish meal, linseed meal and groundnut-protein meal by rumen micro-organisms in vitro were similar to those found in vivo. The rates of hydrolysis of a number of 14C-labelled proteins, including glycoprotein II and lectin from kidney beans (Phaseolus vulgaris), were determined with mixed rumen micro-organisms and with proteases extracted from rumen bacteria. Different soluble proteins were digested at quite different rates, with casein being most readily hydrolysed. Proteins modified by performic acid oxidation, by cross-linking using 1,6-di-iso-cyanatohexane or by diazotization were labelled with 14C. Performic acid treatment generally increased the susceptibility of proteins to digestion, so that the rates of hydrolysis of performic acid-treated proteins were more comparable than those of the unmodified proteins. Cross-linking resulted in a decreased rate of hydrolysis except with the insoluble proteins, hide powder azure and elastin congo red. Diazotization had little effect on the rate of hydrolysis of lactoglobulin and albumin, but inhibited casein hydrolysis and stimulated the breakdown of gamma-globulin.

Targeting of c-myc and beta-globin coding sequences to cytoskeletal-bound polysomes by c-myc 3' untranslated region.

Abstract: The influence of the 3' untranslated region on mRNA localization was investigated by measuring the distribution of myc, beta-globin and hybrid myc-globin mRNAs between free, cytoskeletal-bound and membrane-bound polysomes in cells transfected with either control or chimeric gene constructs. c-myc sequences and beta-globin-coding sequences linked to the myc 3' untranslated region were present at greatest enrichment in cytoskeletal-bound polysomes. beta-Globin mRNA and myc-coding sequences linked to the beta-globin 3' untranslated region were recovered largely in the free polysomes. In situ hybridization confirmed that replacement of the c-myc 3' untranslated region by that of globin caused a relocalization of the mRNA. The results suggest that mRNA localization in differentiated eukaryotic cells depends on a mechanism that involves directional information in the 3' untranslated region of mRNAs.