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  • Polymer and Materials Science  (2)
  • Cell multiplication  (1)
  • 1
    ISSN: 1432-136X
    Keywords: Synthetic nutrient medium ; Cell multiplication ; Hemin ; Phospholipids ; Tetrahymena
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The ciliate Tetrahymena thermophila was grown in a synthetic nutrient medium at various amino acid concentrations. Before the beginning of the experiments the cells were starved for 4 h in a pH buffer. They were inoculated at an initial density of only 250 cells per ml. Under these conditions the cells grew and multiplied at only the two highest amino acid concentrations used. Hemin or phospholipids were found to stimulate cell growth at the lower amino acid concentrations. The mechanism behind this stimulatory effect is unknown, but may be connected with the maintenance of an adequate energy flow under adverse conditions. These additions represent an improvement of the synthetic medium for Tetrahymena.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Pyridoxylated adult human hemoglobin (HbAo) was prepared using a one molar equivalent of pyridoxal 5-phosphate (PLP) per heme and reduced with either NaCNBH3 or NaBH4. A separate sample was pyridoxylated and passed through a mixed-bed ion exchange column without reduction. All three preparations had a P50 of 29 ± 2 torr and a cooperativity of n = 2.4 ± 0.1. These preparations, in both the oxy and deoxy forms, were then treated with 7 equivalents of glutaraldehyde per tetramer at pH 6.8 at 4°C and at room temperature. The polymerization invariably reduced the P50 to 18 ± 2 torr with Hill coefficients of less than 2. These solutions, with or without further reduction using NaCNBH3, all retained the PLP in differing amounts (2-3 moles/tetramer). Methemoglobin concentrations were increased during the polymerization reaction. The normal pyridoxylation procedure, using sodium borohydride reduction, resulted in a number of different molecular species. Polymerization with glutaraldehyde caused a further proliferation of molecular species that could not be separated by anion exchange chromatography or by isoelectric focusing. The extent of polymerization, estimated by gel exclusion chromatography and SDS polyacrylamide gel electrophoresis, was from 40 to 50%. Analysis of the reverse phase chromatograms, which separate the heme and the α- and β-chains, showed extensive polymerization and distribution of the radioactively labeled PLP on the protein for all preparations. All of the polymerized and pyridoxylated samples were unstable, and showed different chromatographic patterns after storage at 4°C for 1 month. Attempts to stabilize these preparations by further reduction with NaCNBH3 gave products with a lower P50 and lower cooperativity. When the reactions were conducted with a purified HbAo, heterogeneity was somewhat decreased compared to the normally used stroma-free hemoglobin, but a large number of molecular species were still formed.
    Additional Material: 8 Ill.
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  • 3
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A number of chemically modified hemoglobin preparations have been proposed for use as an emergency resuscitation fluid. The purpose for forming these hemoglobin derivatives is to decrease the oxygen binding (i.e., to increase the P50) and to increase the intravascular retention time. These goals have been met with various degrees of success by using the reaction with pyridoxyl 5-phosphate to raise the P50, followed by the addition of glutaraldehyde to increase circulating half-life by polymerization.1,2 Other derivatives have been formed with polyethylene glycol,3,4 bis-(3,5-dibromosalicyl) fumarate,5,6 glycolaldehyde,7 and 2-nor-2-formylpyridoxal 5-phosphate,8,9 as well as with other compounds. All these derivatives introduce a foreign molecule into the hemoglobin, which may not always be desirable. Recently Tharp and Day10 used cyanogen to form intersubunit amide cross-links in hemoglobin without the incorporation of cyanogen. This approach is attractive if the appropriate functional properties can be attained. Takeda et al.11 showed that equimolar concentrations of amino acids and disuccinimidyloxalate could form peptide bonds in high yield. We report the characteristics of the hemoglobin molecule modified by internal covalent amide bonds, which may be a suitable candidate for a resuscitation fluid.
    Additional Material: 3 Ill.
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