This report explains the concepts and field methods to be used by the U.S. Geological Survey's National Water-Quality Assessment (NAWQA) Program for evaluating contaminants in tissues of biological organisms. Laboratory methods for analysis of these contaminants will be detailed in a future report. Part 1 explains the rationale for analyzing contaminants in tissues and gives an overview of the approach. Part 2 describes the tissue-contaminant strategies of other agencies and compares them to the strategy used in NAWQA. Part 3 details the approach for the use of tissue analysis as an aid to interpreting quality of water in NAWQA study units. Concentrations of contaminants in tissues will complement measures of water and sediment chemistry, and ecological surveys in NAWQA, providing multiple lines of evidence for waterquality assessments. Individual sections in Part 3 provide detailed discussions of target contaminants, target taxa, and field procedures. Suggestions for interpretation of data are presented to facilitate consistency among NAWQA study units. Purpose and Scope This document describes the rationale, objectives, approach, and procedures to be used in the NAWQA Program for determining the occurrence, distribution, and trends in concentrations of trace elements and synthetic organic compounds in tissues (termed here tissue-contaminant studies). It is recognized that at least some of these approaches will evolve as additional experience is gained and as measurement and analysis techniques advance.
This review recollects literature data on sensitivity and dynamic range for the most commonly used colorimetric and fluorescent dyes for general protein staining, and summarizes procedures for the most common PTM-specific detection methods. It also compiles some important points to be considered in imaging and evaluation. In addition to theoretical considerations, examples are provided to illustrate differential staining of specific proteins with different detection methods. This includes a large body of original data on the comparative evaluation of several pre-and post-electrophoresis stains used in parallel on a single specimen, horse serum run in 2-DE (IPG-DALT). A number of proteins/protein spots are found to be over-or under-revealed with some of the staining procedures.
Despite calls for performance-oriented and evidence-based planning, the outcomes of land use and environmental plans are rarely monitored or assessed ex post facto (that is, post implementation). As a result, planners cannot know whether or why plans achieve their goals, or learn from the results of past interventions to improve planning practice. This evaluation gap is caused by a lack of methodology to evaluate the outcomes of plans and the difficulty of attributing changes to planning activities. We address this gap by proposing and testing a plan-outcome evaluation (POE) methodology. We demonstrate its broad applicability and usefulness in the context of local plans in New Zealand. The POE methodology will be useful to practitioners and academics seeking to assess the outcomes of plans in countries with western planning traditions.
Heterogenous nuclear ribonucleoproteins (hnRNPs) such as hnRNP A1 are tightly associated with heterogenous nuclear RNAs (hnRNAs) within eukaryotic nuclei and are thought to be involved in hnRNA processing and splice site selection. The NH2-terminal two-thirds of hnRNP A1 contains two 92-amino acid RNA binding domains (RBDs) that are arranged in tandem and are more than 30% homologous with each other. Following this region is a flexible glycine-rich COOH-terminal domain. We have studied the nucleic acid binding properties of the two isolated RBDs (residues 1-92 and 93-184, respectively) and of A1 fragments corresponding to residues 1-184 and 1-196 (i.e., the latter fragment is called UP1) in order to evaluate their relative contributions to A1 binding. We have determined that the individual RBDs of A1 bind poly[r(epsilon A)], a fluorescent single-stranded RNA (ssRNA), with a surprisingly low apparent association constant of only 1.5 x 10(4) M-1 (1-92) and 4.5 x 10(4) M-1 (93-184), respectively. We hypothesize that this low affinity represents a basal level of binding that is common to most RBD-containing proteins. Oligonucleotide binding studies suggest the interaction site size for the 93-184 fragment is approximately 4 nucleotides or less and salt sensitivity studies indicate that only about 27% of the free energy of binding of this RBD derives from ionic interactions. Since the affinity of the 1-184 fragment is at least 10-fold above that of either of its component RBDs, both must contribute to binding. This conclusion is further supported by the increased occluded site size of 1-184 (n = 14 +/- 2), as compared to its 93-184 RBD (n = 6 +/- 1), and by the biphasic binding that was observed for the UP1:poly(U) interaction at pH 6.0. Our finding that the affinity of the 1-184 fragment is 1000-fold less than the product of the affinities of its 1-92 and 93-184 RBDs is consistent with these domains being joined by a flexible linker. By comparing the affinities of the 1-184 fragment with that for A1, we conclude that together the two RBDs in A1 account for only 53% of the free energy of A1 binding. Comparative binding studies with UP1 demonstrate that the short region spanning residues 185-->195 represents an important determinant of the binding affinity of A1 and, since this region contains a site of dimethylation, it may provide a mechanism for regulating the affinity of A1 for specific nucleic acid targets.
Understanding the role of drinking games in college student life is critical for program planners who wish to develop education and prevention programs to reduce abusive drinking. Drinking games are popular social activities that provide a focus for social interactions but place students at considerable risk for serious consequences. This article reports preliminary results of a study using participant observation and in-depth interviews to develop a typology of drinking games and describe patterns and practices associated with the games.
New mass-tagging reagents for quantitative proteomics measurements have been designed using solid phase peptide synthesis technology. The solid phase mass tags have been used to accurately measure the relative amounts of cysteine-containing peptides in model peptide mixtures as well as in mixtures of tryptic digests in the femtomol range. Measurements were made using both matrix-assisted laser desorption ionization-time-of-flight mass spectrometry (MALDI-TOF MS) and online reversed-phase capillary liquid chromatography coupled through a nanoelectrospray interface to an ion trap mass spectrometer (capillary LC/ESI-MS). Results of mass-tagging experiments obtained from these two mass spectrometry techniques and their relative advantages and disadvantages for identification and quantitation of mass tagged peptides are compared. These reagents provide a simple, rapid and cost-effective alternative to currently available mass tagging technologies.
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