A plan for administrative computing at ANL FY1991 through FY1993

In July of 1988, Argonne National Laboratory management approved the restructuring of Computing Services into the Computing and Telecommunications Division, part of the Physical Research area of the Laboratory. One major area of the Computing and Telecommunications Division is Management Information Systems (MIS). A significant aspect of Management Information Systems' work is the development of proposals for new and enhanced administrative computing systems based on an analysis of informational needs. This document represent the outcome of the planning process for FY1991 through FY1993. The introduction of the FY1991 through FY1993 Long-Range Plan assesses the state of administrative computing at ANL and the implications of FY1991 funding recommendations. It includes a history of MIS planning for administrative data processing. This document discusses the strategy and goals which are an important part of administrative data processing plans for the Laboratory. It also describes the management guidelines established by the Administrative Data Processing Oversight Committee for the proposal and implementation of administrative computing systems. Summaries of the proposals for new or enhanced administrative computing systems presented by individual divisions or departments with assistance of Management Information Systems, to the Administrative Data Processing Oversight Committee are given. The detailed tables in this paper give information on how much the resources to develop and implement a given systems will cost its users. The tables include development costs, computing/operations costs, software and hardware costs, and efforts costs. They include both systems funded by Laboratory General Expense and systems funded by the users themselves

Phosphorylation of caldesmon by myosin light chain kinase increases its binding affinity for phosphorylated myosin filaments

Phosphorylation of myosin by myosin light chain kinase (MLCK) is essential for smooth muscle contraction. In this study we show that caldesmon (CaD) is also phosphorylated in vitro by MLCK. The phosphorylation is calcium- and calmodulin (CaM)-dependent and requires a MLCK concentration close to that found in vivo. On average, approximately 2 mol Pi per mol of CaD are incorporated at Thr-626 and Thr-693, with additional partial phosphorylation at Ser-658 and Ser-702. The phosphorylation rate for CaD is 20- to 50-fold slower than that for filamentous myosin; faster relative rates were obtained with CaD added to purified actomyosin or myosin preparations containing endogenous MLCK/CaM complex. Addition of CaM also augmented CaD phosphorylation. We further demonstrate that [32P] labeled CaD binds much more readily to phosphorylated filamentous myosin than to unphosphorylated myosin. For actomyosin, CaD binding affinity doubles after myosin phosphorylation, without a significant change in binding stoichiometry (approx. one CaD per myosin molecule). Unphosphorylated CaD is ineffective in competing with the phosphorylated protein for the binding site(s) on myosin filaments. The ATPase activity of reconstituted actomyosin is inhibited by unphosphorylated CaD, and this inhibition was removed by CaD phosphorylation. Our results suggest that CaD phosphorylation plays a role in modifying actomyosin interaction in vivo, particularly during prolonged muscle activation