ABSTRACT
Severe anemia in a weanling kitten resulted in volume overload hypertrophy of the heart and signs of congestive heart failure. A 6-week-old moribund kitten was admitted to the hospital with a PCV of 3%. The anemia was determined to have resulted from severe flea infestation and iron deficiency. Supportive therapy consisted of flea removal, blood transfusions, and oral nutritional support. On day 3 of hospitalization, the kitten had signs of depression and became tachypneic. Auscultation revealed a systolic murmur, gallop rhythm, and crackles over the ventral lung fields. Thoracic radiography revealed pulmonary edema and massive cardiomegaly. Echocardiographic evaluation revealed dilatation of all cardiac chambers. The addition of furosemide to the kitten's treatment protocol resulted in resolution of the pulmonary edema. On follow-up examination 1 month later, the kitten had mild residual cardiomegaly and the anemia had resolved. Anemia is a well-known sequela to severe flea infestation in young animals. A less commonly reported, but potentially life-threatening, sequela to anemia may include the development of volume overload hypertrophy of the heart and congestive heart failure.
Subject(s)
Anemia, Hypochromic/veterinary , Cardiomegaly/veterinary , Cat Diseases/etiology , Ectoparasitic Infestations/veterinary , Siphonaptera , Anemia, Hypochromic/complications , Anemia, Hypochromic/etiology , Animals , Cardiomegaly/complications , Cardiomegaly/etiology , Cats , Ectoparasitic Infestations/complications , Female , Heart Failure/etiology , Heart Failure/veterinaryABSTRACT
Agarose is degraded by a beta-agarase from Pseudomonas atlantica to neoagarooligosaccharides of degree of polymerization (DP), 4, 6, 8, and 10. A beta-neoagarotetraose hydrolase cleaves the central beta-linkage in neoagarotetraose and the beta-linkage near the nonreducing end in neoagarohexaose and -octaose to yield neoagarobiose. The beta-neoagarotetraose hydrolase was localized on or outside the cytoplasmic membrane, in the cell wall region. The enzyme was activated by NaCl, KCl, CaCl2, MnCl2, and MgSO4, has a Km of 3.4 X 10(-3) M for neoagarotetraose, was free from beta-agarase and alpha-neoagarobiose hydrolase activity, and showed no transglycosidic activity.
Subject(s)
Galactosidases/isolation & purification , Pseudomonas/enzymology , Agar , Cell Membrane/enzymology , Diazonium Compounds/pharmacology , Enzyme Induction , Galactosidases/biosynthesis , Galactosidases/metabolism , Hydrogen-Ion Concentration , Kinetics , Sodium Chloride/pharmacologyABSTRACT
The mixture of polysaccharides in the gelling component of agar (agarose) is hydrolyzed to D-galactose and 3,6-anhydro-L-galactose by a series of hydrolytic enzymes obtained from Pseudomonas atlantica. The final degradative step in the pathway of agarose decomposition is the hydrolysis of the alpha-linkage in the dissaccharide neoagarobiose yielding D-galactose and 3,6-anhydro-L-galactose. Pseudomonas atlantica when grown on agar produces two specific enzymes, p-nitrophenyl alpha-galactose hydrolase and neoagarobiose hydrolase. The purification and partial characterization of both enzymes are presented.
Subject(s)
Agar/metabolism , Glycoside Hydrolases , Pseudomonas/enzymology , Ammonium Sulfate , Cell Membrane/enzymology , Cell-Free System , Chemical Precipitation , Glycoside Hydrolases/isolation & purification , Glycoside Hydrolases/metabolism , Hydrogen-Ion Concentration , Hydrolysis , Lithium/pharmacology , Molecular Weight , Nitrophenylgalactosides/metabolism , Polysaccharides , Potassium/pharmacology , Pseudomonas/metabolism , Seawater , Sodium/pharmacology , Water MicrobiologyABSTRACT
A p-nitrophenyl alpha-galactoside hydrolase is partially released when whole cells of Pseudomonas atlantica are converted to spheroplasts. The p-nitrophenyl alpha-glactoside hydrolase is completely inactivated by treatment of whole cells with diazonaphthalene -- disulfonic acid (NDS), a reagent which does not penetrate the cytoplasmic membrane. Under the conditions used no inactivation of lactic acid dehydrogenase was observed. A specific staining procedure for this enzyme for use in electron microscopy was developed. The results with this technique in conjunction with the results of spheroplasting and NDS localization suggest that p-nitrophenyl alpha-galactoside hydrolase is located in or on the double-track membranes, primarily on the outer double track.
