Mortality due to a retained circle hook in a longfin mako shark Isurus paucus (Guitart-Manday).

A female longfin mako shark Isurus paucus (Guitart-Manday, 1966) was found moribund on the Atlantic Ocean beach near Canaveral National Seashore, Florida; the shark died shortly after stranding. Macroscopic lesions included a partially healed bite mark on the left pectoral fin, a clefted snout, pericardial effusion and a pericardial mass surrounding a 12/0 circle fishing hook. The heart, pericardial mass, gills, ovary, oviduct, shell gland, epigonal organ, liver, kidney and intrarenal and interrenal glands were processed for histopathology and examined by brightfield microscopy.

Biphasic protonation of hydrophilic cargo agents in unilamellar phospholipid vesicles: implications about cargo location.

The commonly used cargo agents for liposome entrapment, chromate and 5(6)-carboxyflourescein (CF), have been sequestered in small unilamellar vesicles composed of dipalmitoylphosphatidylcholine through preparations involving either sonication or extrusion methods. Once loaded, these water-soluble chromophoric cargo agents have been exposed to small quantities of externally applied acid solution, which decreases the pH from neutral to approx. 6.

The interaction of oxymyoglobin with hydrogen peroxide: a kinetic anomaly at large excesses of hydrogen peroxide.

The reaction of oxymyoglobin (MbO2) with H2O2 has been examined at pH 7.2 and 20(+/- 2) degrees C for reactant ratios of [H2O2]:[MbO2] greater than approximately 15:1. Under the conditions of large excesses of H2O2, the reaction is characterized by an increase in the rate of loss of MbO2 as [H2O2] is increased, for which a value of k(MbO2 + H2O2) approximately 3 M-1 s-1 is obtained.

The interaction of oxymyoglobin with hydrogen peroxide: the formation of ferrylmyoglobin at moderate excesses of hydrogen peroxide.

The reaction of oxymyoglobin with H2O2 has been examined at pH 7.2 and 20(+/-2) degrees over a range of [H2O2] up to an initial excess of 25:1. The reaction is characterized by a direct conversion of oxymyoglobin to ferrylmyoglobin without the intermediacy of the ferri derivative.

Interaction of radiation-generated radicals with myoglobin in aqueous solution. III. Effects of oxygen and catalase on the product distribution in solutions of ferrimyoglobin containing N2O.

The gamma-radiolysis of aqueous solutions of ferrimyoglobin in the presence of N2O at pH 7.3 has been examined as a function of added catalase and oxygen. Changes in the nature of the heme group have been monitored by visible absorption spectrophotometry and analysed quantitatively by a multiple wavelength method based on Beer's Law.