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PbS nanocrystals (NCs) are synthesized in aqueous phase within a temperature range of 40-80°C in the presence of native and denatured states of bovine serum albumen (BSA) as the capping/stabilizing agent The NCs are characterized with the help of field-emission scanning electron microscopy, high-resolution transmission electron microscopy, X-ray diffraction, and energy-dispersive X-ray analysis. At40°C, large ball-shaped NCs (145 ± 37 nm) with small surface protrusions are formed when 1 x 10 -4 g mL -1 BSA is used. As the reaction temperature is increased towards 80°C, the size of NCs decreases and they acquire somewhat cubic geometries (49.1 ± 7.0 nm) due to a change in the capping behavior of BSA between its native and denatured states. The native and denatured states of BSA are simultaneously studied by fluorescence spectroscopy using tryptophan emission, and pH measurements with respect to time and temperature. Gel electrophoresis is used to determine the polarity ofthe BSA capped NCs. Only the small sized NCs conjugated with relatively larger amounts of BSA show a displacement towards the positively charged electrode in comparison to larger NCs with lower amounts of BSA capping. It was concluded that the denatured state of BSA is more effective in controlling the crystal growth of PbS than its native state especially in the low concentration range.

Bovine surfactant proteins B (SP-B) and C (SP-C) were analyzed by nano-electrospray ionization mass spectrometry (nano-ESI-MS). The observed molecular masses showed discrepancies compared to the calculated molecular masses using the published amino acid sequences. The number of cysteine residues in the published bovine SP-B amino acid sequences also failed to match the observed mass shift upon reduction of the SP-B dimer. To determine the amino acid sequences of two proteins, SP-B was first digested with trypsin and analyzed by liquid chromatography/tandem mass spectrometry (LC/MS/MS), while SP-C was analyzed by MS/MS in its intact form. The amino acid sequence of bovine SP-B determined here matches the observed molecular mass. The sequence is almost identical to the sheep SP-B except for two amino acid residues, consistent with the proximity of the two species. The correct sequence contains seven cysteine residues. Bovine SP-B exists as dimers and all cysteines are oxidized to form disulfide bonds in physiological conditions, which is in agreement with the observed mass shift upon reduction of the SP-B dimer. These cysteine residues are completely conserved across all species indicating their importance for the biological functions of this surfactant protein. The sequence of SP-C determined here also reveals an L to V substitution at its position 22 compared with the published bovine SP-B sequence.

Surfactant administration causes a rapid and dramatic improvement in gas exchange, but paradoxically, studies have failed to show an improvement in the mechanical properties of the lung. We have measured dynamic and static (passive flow-volume technique) compliance before and after a single dose of bovine lipid extract surfactant in 22 premature infants with RDS. This had no effect on the measured dynamic compliance. In contrast, surfactant significantly increased static compliance from 0.41 ± 0.02 to 0.55 ± 0.04 mL/cm H2,O/kg. This improvement was the result of a substantial recruitment of lung volume after surfactant administration. This led us to reduce ventilator pressures, which produced an increase in both dynamic and static compliance, but did not recruit additional volume. We conclude that surfactant causes a substantial increase in static compliance due to volume recruitment, which is consistent with reports of increase in the measured FRC. However, despite this improvement, the compliance is still below our normal range. © 1993 Wiley-Liss, Inc.

A phospholipase A2 activity associated with the microsomal fraction of rabbit lung homogenates was studied. The enzyme showed specificity for the sn-2 ester bond of phosphatidylcholine, had an alkaline pH optimum and required Ca2+ for activity. Other divalent cations were unable to support hydrolysis. In the absence of detergents, exogenous phosphatidylethanolamine was deacylated at a rate sevenfold higher than phosphatidylcholine. The activity toward both substrates could be enhanced by sodium deoxycholate or, more effectively, by sodium taurodeoxycholate. Phosphatidylethanolamine required higher detergent/phospholipid molar ratios than phosphatidylcholine. Under these conditions, the preference for the former substrate over the latter was nearly abolished. The zwitterionic detergent 3-[(3-cholamidopropyl) dimethylammonio]-1-propanesulfonate (CHAPS) and the nonionic detergent Triton X-100 were either ineffective (phosphatidylcholine) or inhibitory (phosphatidylethanolamine). Addition of KCl produced opposite effects on the activity depending on the bile salt used to disperse the substrate. The phospholipase A2 activity was inhibited by p-bromophenacyl bromide but remained unaffected after treatment with diisopropylfluorophosphate or NaF. N-Ethylmaleimide, but not other thiol reagents, partially inhibited the activity.