Treatment outcomes after combination interventional and cognitive motivational counseling on analgesic medication use in patients with chronic spine pain.

Background: Pain interventionists can interrupt pain through anesthetic blockade of neural transmission to virtually any part of the body. Temporary pain relief can be achieved by the direct application of targeted anesthetic. Diagnostically, nerve blocks help identify specific pain generators, refine differential diagnosis, and disrupt the neural transmission mechanisms to stop pain generation peripherally.

Disulfide bond reduction: A powerful, chemical probe for the study of structure-function relationships in the hemocyanins.

The copper-containing hemocyanins are a class of oxygen-transport proteins whose structures differ in arthropods and molluscs. Crystal structure analyses and amino acid sequence comparisons show that disulfide bonding is a common feature in both arthropod and mollusc hemocyanins. Reduction of the disulfide bonds of a representative set of arthropod and mollusc hemocyanins results in complete loss of their oxygen-binding capacities.

Outcomes of sudden cardiac arrest treated with defibrillation by emergency medical technicians (EMT-Ds) or paramedics in a two-tiered urban EMS system.

Objective: Controversy exists as to the effectiveness of defibrillation by emergency medical technicians (EMT-Ds) in reducing mortality from cardiac arrest in two-tiered EMS systems. This study was performed to assess the impact of EMT-Ds on outcome of sudden cardiac death in a small, urban, modified two-tiered EMS system.

Methods: This was a retrospective, unmatched case-control study comparing the outcomes of patients suffering sudden cardiac death treated by EMT-Ds with paramedic (EMT-P) backup with the outcomes of patients treated by EMT-Ps as first responders.

Active-site disruption in native Limulus hemocyanin and its subunits by disulfide-bond reductants: a chemical probe for the study of structure-function relationships in the hemocyanins.

The crystal structure analysis of Subunit II of Limulus hemocyanin has shown that its polypeptide chain is folded into three distinct structural domains. The oxygen-binding, dinuclear copper center is located deep in the core of Domain 2. Two disulfide bonds are located in a bridging domain, Domain 3.

Xanthine oxidase: an efficient promoter of the iron loading of apoferritin.

Xanthine oxidase exhibits ferroxidase activity and previously has been shown to catalyze the oxidative incorporation of iron into apotransferrin, the iron transport protein of plasma. These studies demonstrate that xanthine oxidase also efficiently promotes the oxidative incorporation of iron into apoferritin, the major iron storage protein of vertebrates, and that the ferroxidase activity of intestinal xanthine oxidase could be important in determining the fraction of iron within the intestinal mucosa cell partitioned to ferritin versus the iron that remains in a transient pool for rapid transport to plasma.