ABSTRACT
We have seen increasing numbers of children who present with serious burns related to camping and outdoor cooking, prompting this 5-year review. Of 34 children (21 boys and 13 girls), with an average age of 5.2 years (4 months to 17 years) and average burn size of 15% (1% to 98%) cared for (4 as outpatients and 30 as inpatients), there was one fatality (3%). Mechanisms of injury included falling into free pits, throwing flammables into grills or pits, placing hands on hot objects in or near a fire, walking or falling into hot embers from an extinguished fire, spills from insect repellant candies, tent fires, burning of paper eating utensils, and cooking scalds. We have initiated a directed prevention program with the regional state park systems.
Subject(s)
Accident Prevention , Burns/epidemiology , Burns/prevention & control , Camping , Cooking , Adolescent , Burns/etiology , Child , Child Welfare , Child, Preschool , Female , Humans , Incidence , Infant , Male , Retrospective StudiesABSTRACT
L-Mandelate dehydrogenase was purified from Acinetobacter calcoaceticus by Triton X-100 extraction from a 'wall + membrane' fraction, ion-exchange chromatography on DEAE-Sephacel, (NH4)2SO4 fractionation and gel filtration followed by further ion-exchange chromatography. The purified enzyme was partially characterized with respect to its subunit Mr (44,000), pH optimum (7.5), pI value (4.2), substrate specificity and susceptibility to various potential inhibitors including thiol-blocking reagents. FMN was identified as the non-covalently bound cofactor. The properties of L-mandelate dehydrogenase are compared with those of D-mandelate dehydrogenase, D-lactate dehydrogenase and L-lactate dehydrogenase from A. calcoaceticus.
Subject(s)
Acinetobacter/enzymology , Alcohol Oxidoreductases/metabolism , Alcohol Oxidoreductases/antagonists & inhibitors , Alcohol Oxidoreductases/isolation & purification , Cell Membrane/enzymology , Flavin Mononucleotide/metabolism , L-Lactate Dehydrogenase/metabolism , Molecular Weight , UltrasonicsABSTRACT
Acinetobacter calcoaceticus possesses an L(+)-lactate dehydrogenase and a D(-)-lactate dehydrogenase. Results of experiments in which enzyme activities were measured after growth of bacteria in different media indicated that the two enzymes were co-ordinately induced by either enantiomer of lactate but not by pyruvate, and repressed by succinate or L-glutamate. The two lactate dehydrogenases have very similar properties to L(+)-mandelate dehydrogenase and D(-)-mandelate dehydrogenase. All four enzymes are NAD(P)-independent and were found to be integral components of the cytoplasmic membrane. The enzymes could be solubilized in active form by detergents; Triton X-100 or Lubrol PX were particularly effective D(-)-Lactate dehydrogenase and D(-)-mandelate dehydrogenase could be selectively solubilized by the ionic detergents cholate, deoxycholate and sodium dodecyl sulphate.
