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- BookElizabeth Stepp Gilbert.Summary: As the only book of its kind, this text provides a complete resource for care of the high risk patient and her complex needs. It helps you provide the best care and increase positive outcomes with coverage of today's newest technology, physiologic considerations, psychologic implications, health disorders, and other complications in pregnancy. This book also describes how to screen for risk factors, provide preventive management, and intervene appropriately when problems arise. It's a concise, hands-on reference for both inpatient and outpatient settings. --Book Jacket.
Contents:
Physiologic and nutritional adaptations to pregnancy
General nursing assessment of the high risk expectant family
Assessment of fetal well-being
Perinatal screening, diagnoses, and fetal therapies
Integrative therapies in pregnancy and childbirth
Psychologic adaptations
Perinatal death and bereavement care
Ethical decision making
Legal issues and risk management
Diabetes
Cardiac disease
Renal disease
Autoimmune rheumatic diseases
Venous thromboembolic disease
Pulmonary disease and respiratory distress
Spontaneous abortion
Ectopic pregnancy
Gestational trophoblastic disease
Placental abnormalities
Disseminated intravascular coagulation
Hemolytic incompatibility
Hypertensive disorders
Preterm labor and multiple gestation
Premature rupture of membranes
Trauma
Sexually and nonsexually transmitted genitourinary infections
Substance abuse
Labor stimulation
Dysfunctional labor
Prolonged pregnancy.Digital Access ClinicalKey Nursing 2011 - ArticledeHaseth PL, Lohman TM, Burgess RR, Record MT.Biochemistry. 1978 May 02;17(9):1612-22.We have investigated the nonspecific interactions of Escherichia coli RNA polymerase core and holoenzyme with double-stranded (ds) and single-stranded (ss) DNA. Binding constants for these interactions as functions of such solution variables as monovalent and/or divalent cation concentration, temperature, or pH were determined by the method of deHaseth et a. [deHaseth, P.L., Gross, C.A., Burgess, R.R. and Record, M.T. (1977), Biochemistry 16, 4777--4783] from analysis of the elution of the proteins from small columns containing immobilized DNA. This technique, although as yet empirical, has been demonstrated to yield accurate binding constants fot the nonspecific interation of lac repressor with ds DNA. We find that observed binding constants (Kobsd) are extraordinarily sensitive functions of the monovalent cation concentration for the interactions of both core and holoenzyme with ds DNA. In the absence of divalent cations, the derivatives --(d log Kobsd/d log [Na+]) are 11 +/- 2 for the holo--ds DNA interaction and 21 +/- 3 for the core--ds DNA interaction. Consequently, approximately 11 and 21 low-molecular-weight ions are released, iin the thermodynamic sense, in the formation of the holo--ds and core--ds complexes, respectively (Record, M.T., Jr., Lohman, T.M., and deHaseth, P.L. (1976), J. Mol. Biol. 107, 145--158; Record, M.T., Jr., Anderson, C.F., and Lohman, T.M. (1978), Q. Rev. Biophys., in press). Ion release is a thermodynamic driving force for these nonspecific interactions and causes the stability of the complexes to increase very substantially with a reduction in monovalent ion concnetration. Possible molecular models which account for the different salt sensitivities of the holo--ds and core--ds complexes are discussed. Effects of the competitive ligand Mg2+ on these interactions are also examined. Substantial ion release (approximately 18 monovalent ions) also accompanies the interaction of either holo or core polymerase with ss DNA. Over the range of ion concentrations investigated the holo--ss interaction is substantially stronger than the core--ss interaction; furthermore, we conclude that the interactions of polymerase with ss DNA are, in general, stronger than the nonspecific interations of the enzyme with ds DNA. It is likely that the nonspecific interactions of RNA polymerase with DNA have physiological relevance. Not only is it plausible to assume that the same regions of the protein are involved in both specific and nonspecific interactions, but in addition nonspecific interactions of RNA polymerase and DNA may play role in determining the availability of this protein, in both the thermodynamic and the kinetic sense, for promoter binding and RNA chain initiation [von Hippel. P.H., Revzin, A., Gross, C.A., and Wang, A.C. (1974), Proc. Natl. Acad. Sci U.S.A. 71, 4808--4812]. Consequently, the strong dependences of the nonspecific interactions of RNA polymerase on ionic conditions suggest the possibility of a modulating role of ion concentrations in the control of transcription.