Developing a Chemical Hygiene Plan - American Chemical Society

(in Washington, D.C. 872*4363) and use your credit card! from the CZE-supporting electrolyte. Smith suggested that the development of isotachophoresis...
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Developing a Chemical Hygiene Plan

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his essential "how-to" book tells you what you need to know to comply with the federal regulation known as the "OSHA Laboratory Standard" which requires chemical hygiene plans. Developed by the ACS Committee on Chemical Safety, the guide pre­ sents hygiene plans that can be modified ac­ cording to the particulars of individual labora­ tories. Among the topics covered in this valuable book you'll find • application of the OSHA Laboratory Standard • history of the OSHA Laboratory Standard • standard operating procedures

• control measures and equipment • records and recordkeeping In addition, several appendices are provided, including employee information and training techniques, exposure assessment procedures, the elements of an emergency procedure plan, the OSHA Laboratory Standard, a list of con­ tacts for states that have OSHA-approved state plans, and a list of acronyms. This reference is critical to all lab supervi­ sors who must have in place by January 31, 1991, a chemical hygiene plan that outlines specific work practices and procedures ensur­ ing employee protection from health hazards associated with hazardous chemicals. by Jay A. Young, Warren K. Kingsley, and George H. Wahl Developed by the Committee on Chemical Safety of the American Chemical Society 72 pages (1990) Paperbound ISBN 0-8412-1876-5 LC 90-46721 $18.95 American Chemical Society Distribution Office, Dept 87 1155 Sixteenth St., N.W. Washington, DC 20036 or CALL TOLL FREE

800-227-5558 (in Washington, D.C. 872-4363) and use your credit card!

from the CZE-supporting electrolyte. Smith suggested that the development of isotachophoresis/ES MS might over­ come the problems caused by the elec­ trolyte. He projected that improved MS interfacing techniques may begin to fulfill the increasing demand for in­ formation regarding the microheterogeneity of biomolecular species. Evan Williams from Stanford Uni­ versity presented a unique combina­ tion of CZE and pulsed laser ionization, which used the continuous ice forma­ tion witnessed at the end of the CZE tip. He found that biomolecular species could be ablated from the ice into the gas phase and laser ionized. Following the laser pulse, the ice reforms, and the next sample can be ablated, thus cou­ pling the intrinsic continuous-flow op­ eration of CZE with the pulsed nature of a laser system. Ken Busch of the Georgia Institute of Technology has accessed species of even greater mass (up to «100 000 Da) than those analyzed thus far by CZE by developing a new interface between planar gel electrophoresis and continu­ ous-flow fast atom bombardment (FAB) MS. The interfacing of supercritical fluid chromatography (SFC) and MS is seen as another new area of research. Susan Olesik of The Ohio State University in­ vestigated the energetics of the cluster ions formed in the jet expansion region of a combined SFC/field-enhanced ionization MS interface. Based on her studies, Olesik predicts that it will be possible to control the internal energy of the cluster ions—and thus the subse­ quent degree of fragmentation—by scanning through the phase transition region of the supercritical fluid carrier. Molecular weight and spectral repro­ ducibility problems arise because of difficulties in reproducing restricter cone tips. Olesik was able to overcome these limitations with improved ma­ chining technology. The analysis of large biomolecules will be facilitated by the successful in­ terfacing of ESI with FT-ICR (ESF T M S ) , presented by Kent Henry from Cornell University (7). The ex­ tremely high resolution afforded at low ml ζ (< 3000) permits accurate isotopic 13 C peak assignments. This may pro­ vide a means of assigning masses to multiply charged fragment ions follow­ ing MS/MS biomolecules in an FTICR mass spectrometer. Unraveling the mechanism of the ionization of large molecules in these new interface regions, as well as in ES, secondary ion mass spectrometry (SIMS), FAB, and LD, continues to be an active area of research. Kelsey Cook of the University of Tennessee studied

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the effect of changes in the sample ma­ trix of electrohydrodynamically ion­ ized mono- and di-quaternary ammo­ nium salts to model the solution pro­ cesses that may be occurring in FAB and SIMS. These processes are diffi­ cult to monitor directly with these techniques because of interferences from the primary atom beam (8). Jerry H u n t of Argonne National Laboratory probed the axial and radial energy distributions of a variety of ions formed by LD and photoionization in a TOF mass spectrometer by imaging the ions with a position-sensitive detector. The velocity distributions of the ions were on the order of 1 eV. Williams also reported the use of a vapor-deposited P t resistance thermom­ eter to measure the temperature of a quartz surface during nonmatrixassisted LD. The temperatures were found to be in good agreement with theoretical calculations on the same surface (9). An important conclusion of Michael Ikonomou's investigation into the mechanism of ES and ion spray ioniza­ tion at the University of Alberta is that droplet charging occurs at the sprayer tip and not as the droplet travels toward the counterelectrode (10). These and other studies presented at the symposium indicate that rapid pro­ gress is being made in understanding the mechanisms of biomolecular ion­ ization. Chemical reactions in analytical MS The study and use of chemical reac­ tions—in both the gas and solution phases—is becoming increasingly widespread in analytical MS. Under­ standing gas-phase ion-molecule pro­ cesses in an effort to manipulate the chemistry either before or after the mass spectrometric step is extending the analytical capabilities of MS. Jon Amster at the University of Georgia selectively varied the exothermicity of the chemical ionization reac­ tion of a laser-desorbed dipeptide (AlaVal) by changing the reagent gas (from NH 3 to C 2 H 4 to N 2 0) to produce in­ creasingly "hotter" ions and in so doing manipulated the fragmentation pat­ tern of the peptide. Scott McLuckey's search for "an an­ alytically useful reaction" at ORNL led to the study of the proton transfer reac­ tion between multiply protonated myoglobin (formed from electrospray with a QIT mass spectrometer) and the bases dimethylamine and 1,6-hexanediamine. The decrease in the charge state of the protein was found to vary as a function of both the proton affinity of the reagent base and the trapping time of the reaction (11). This use of